TRANSGLUTAMINASE MEDIATED CONJUGATION OF PEPTIDES FIELD OF THE INVENTION The present invention relates to a novei method for post-translational conjugation of peptides wherein transglutaminase is used to incorporate a point of attachment in the peptide whereto another group can be selectively attached. Said conjugated peptides have altered characteristics and may thus be of use in therapeutic applications or they may ease the analysis or isolation and purification of said peptides. BACKGROUND OF THE INVENTION It is well-known to modify the properties and characteristics of peptides by conjugat-ing groups to the peptide which duly changes the properties of the peptide. Such conjugation generally requires some funcţional group in the peptide to react with another funcţional group in a conjugating group. Typically, amino groups, such as the N-terminal amino group or the e-amino group in lysines, have been used in combination with a suitable acylating reagent. It is often desired or even required to be able to control the conjugation reaction, i.e. to control where the conjugating compounds are attached and to control how many conjugating groups are attached. This is often referred to as specificity. It is an object of the present invention to provide a method by which peptides may be conjugated with a high degree of specificity. In general terms, the method exploits an en-zyme, e.g. transglutaminase, capable of incorporating a compound comprising a suitable funcţional group into the peptide, where said funcţional group is subsequently used as a point where to conjugate. Conjugation of peptides in general has been known for a long time, and US 4,179,337 disclosed more than 20 years ago peptides conjugated to polyethylene or poly-propylene glycols. Different types of chemistries have been disclosed which are effective in forming a bond between the peptide and the moiety to be conjugated to the peptide. EP 605 963 dis-closes the grafting of aqueous polymers which form an oxime linkage with an aldehyde group on a protein. None of the natural amino acid comprises an aldehyde, so a hydroxyl group thus has to be oxidized as a first step in the conjugating process. WO 96/41813 discloses polymers which are functionalised with an amino-oxy oxime forming group useful in conjugation reactions. WO 98/05363 discloses a compound comprising a peptide and a water- soluble polymer, wherein the two are covalently bonded through an oxime bond at the N-terminal amino acid residue. Furthermore, the use of enzymes to enable a more specific conjugation of peptides is known. EP 243 929 discloses the use of proteolytic enzymes, such as carboxypeptidase to incorporate a compound with a funcţional group in the C-terminal of a peptide, where said funcţional group can subsequently be used as a point where to attach cytotoxic groups, other peptides or reporter groups used to facilitate analysis of the peptide, such as e.g. fluorescent groups. This technique, however, limits the point of attachment to the C-terminal amino acid residue, something which constituie a severe limitation if the C-terminal residue is essential for the activity of the peptide. Transglutaminase has previously been used to alter the properties of peptides. In the food industry and particular in the diary industry many techniques are available to e.g. cross-bind peptides using transglutaminases. Other documents disclose the use of transglu-taminase to alter the properties of physiologically active peptides. EP 950665, EP 785276 and Sato, Adv. Drug Delivery Rev., 54, 487-504, 2002 disclose the direct reaction between peptides comprising at least one Gin and amine-functionalised PEG or similar ligands in the presence of transglutaminase, and Wada in Biotech. Lett., 23,1367-1372, 2001 discloses the direct conjugation of p-lactoglobulin with fatty acids by means of transglutaminase. SUMMARY OF THE INVENTION The present inventors have surprisingly found that enzymes, such as e.g. transglutaminase may be used to incorporate into a peptide one or more funcţional groups, which are not accessible in the in the peptide to form a functionalised peptide, and that this functional-ised peptide may subsequently be reacted with another compound comprising a conjugating moiety and one or more funcţional groups capable of reacting with the funcţional group or groups thus incorporated in the peptide but not with other funcţional groups present in the peptide. Such method provides a high degree of specificity in that transglutaminase can only catalyse the incorporation of compounds at amino acid residues which are substrates for transglutaminase, and in that the funcţional groups are selected so that they only react with each other, not with other funcţional groups accessible in the peptide. In this way, the conjugating moiety is only attached at controlled locus or loci, and by selecting the funcţional groups, the number of conjugated groups can be controlled. Accordingly, in one embodiment, the present invention provides a method for conjugating peptides, said method comprising the steps of i) reacting in one or more steps a peptide with a first compound comprising one or more funcţional groups or latent funcţional groups, which are not accessible in any of the amino acids consti-tuting said peptide, in the presence of transglutaminase capable of catalysing the incorporation of said first compound into said peptide to form a functionalised peptide, and ii) optionally activate said latent funcţional group, and iii) reacting in one or more steps said functionalised peptide with a second compound comprising one or more funcţional groups, wherein said funcţional group(s) do not react with funcţional groups accessible in the amino acid residues constituting said peptide, and wherein said funcţional group(s) in said second compound is capable of reacting with said funcţional group(s) in said first compound so that a covalent bond between said functionalised peptide and said second compound is formed. It is also an objective of the present invention to provide peptides conju-gated by the method of the present invention. It is a further objective of the present invention to provide peptides which are modified in a way to make them better suited for the method of the present invention. It is a still further objective of the present invention to provide reagents and enzymes suitable for use in the methods of the present invention. It is a still further objective of the present invention to provide compositions, e.g. pharmaceutical compositions comprising peptides conjugated by methods of the present invention. It is a still further objective of the present invention to provide peptides conjugated according to the methods of the present invention for use in therapy. It is a still further objective of the present invention to provide therapeutic methods for the treatment of diseases comprising the administration of conjugated peptides prepared according to the methods of the present invention. It is a still further objective of the present invention to provide a use of conjugated peptides prepared according to the methods of the present invention in the manufacture of medicaments. It is a still further objective of the present invention to provide a method for improving the pharmacological properties of a peptide by conjugation said peptide according to the methods of the present invention. DEFINITIONS In the present context "transamination" or similar is intended to indicate a reaction where nitrogen in the side chain of glutamine is exchanged with nitrogen from another compound, in particular nitrogen from another nitrogen containing nucelophile. In the present context, the term "not accessible" is intended to indicate that some-thing is absent or de facto absent in the sense that it cannot be reached. When it is stated that funcţional groups are not accessible in a peptide to be conjugated it is intended to indicate that said funcţional group is absent from the peptide or, if present, in some way pre-vented from taking part in reactions. By way of example, said funcţional group could be bur-ied in the structure of the peptide so that it is shielded from participating in the reaction, or it could be located in an area of the peptide where restricted flexibility of the peptide chain pre-vents the funcţional group from participating in reactions. It is recognised that whether or not a funcţional group is accessible depends on the reaction conditions. It may be envisaged that in the presence of denaturing agents or at elevated tempera t u res the peptide may unfold to expose otherwise not accessible funcţional groups. It is to be understood that "not accessible" means "not accessible at the reaction condition chosen for the particular reaction of in-terest". In the present context, the term "oxime bond" is intended to indicate a moiety of the formula -C=N-O-. In the present context, the term "hydrazone bond" is intended to indicate a moiety of the formula -C=N-N-. In the present context, the term "phenylhydrazone bond" is intended to indicate a moiety of the formula (Figure Removed) In the present context, the term "semicarbazone bond" is intended to indicate a moiety of the formula -C=N-N-C(O)-N-. The term "alkane" is intended to indicate a saturated, linear, branched and/or cyclic hydrocarbon. Unless specified with another number of carbon atoms, the term is intended to indicate hydrocarbons with from 1 to 30 (both included) carbon atoms, such as 1 to 20 (both ncluded), such as from 1 to 10 (both included), e.g. from 1 to 5 (both included); or from 15 to 30 carbon atoms (both included). The term "alkene" is intended to a indicate linear, branched and/or cyclic hydrocar-bon comprising at least one carbon-carbon double bond. Unless specified with another num-ber of carbon atoms, the term is intended to indicate hydrocarbons with from 2 to 30 (both included) carbon atoms, such as 2 to 20 (both included), such as from 2 to 10 (both included), e.g. from 2 to 5 (both included); or from 15 to 30 carbon atoms (both included). The term "alkyne" is intended to indicate a linear, branched and/or cyclic hydrocar-bon comprising at least one carbon-carbon triple bond, and it may optionally comprise one or more carbon-carbon double bonds. Unless specified with another number of carbon atoms, the term is intended to indicate hydrocarbons with from 2 to 30 (both included) carbon atoms, such as from 2 to 20 (both included), such as from 2 to 10 (both included), e.g. from 2 to 5 (both included); or from 15 to 30 carbon atoms (both included). The term "homocyclic aromatic compound" is intended to indicate aromatic hydrocarbons, such as benzene and naphthalene. The term "heterocyclic compound" is intended to indicate a cyclic compound comprising 5, 6 or 7 ring atoms from which 1, 2, 3 or 4 are hetero atoms selected from N, O and/or S. Examples of heterocyclic aromatic compounds include thiophene, furan, pyran, pyrrole, imidazole, pyrazole, isothiazole, isooxazole, pyridine, pyrazine, pyrimidine, pyridaz-ine, as well as their partly orfully hydrogenated equivalents, such as piperidine, pirazolidine, pyrrolidine, pyroline, imidazolidine, imidazoline, piperazine and morpholine. The terms "hetero alkane", "hetero alkene" and "hetero alkyne" is intended to indicate alkanes, alkenes and alkynes as defined above, in which one or more hetero atom or group have been inserted into the structure of said moieties. Examples of hetero groups and atoms include -O-, -S-, -S(0)-, -S(O)2-, -C(0)- -C(S)- and -N(R*)-, wherein R* represents hy-drogen or d-Ce-alkyl. Examples of heteroalkanes include. (Table Removed) The term "radical" or "biradical" is intended to indicate a compound from which one ortwo, respectively, hydrogen atoms have been removed. When specifically stated, a radical may also indicate the moiety formed by the formal removal of a larger group of atoms, e.g. hydroxyl, from a compound. The term "halogen" is intended to indicate members of the seventh main group of the periodic table, e.g. F, CI, Br and I. The term "PEG" is intended to indicate polyethylene glycol of a molecular weight be-tween approximately 100 and approximately 1,000,000 Da, including analogues thereof, wherein for instance the terminal OH-group nas been replaced by an alkoxy group, such as e.g. a methoxy group, an ethoxy group or a propoxy group. In particular, the PEG wherein the terminal -OH group has been replaced by methoxy is refered to as mPEG. The term "mPEG" (or more properly "mPEGyl") means a polydisperse or monodis-perse radical of the structura wherein m is an integer larger than 1. Thus, a mPEG wherein m is 90 has a molecular weight of 3991 Da, i.e. approx 4kDa. Likewise, a mPEG with an average molecular weight of 20 kDa has an average m of 454. Due to the process for producing mPEG these molecules often have a distribution of molecular weights. This distribution is described by the polydispersity index. The term "polydispersity index" as used herein means the ratio between the weight average molecular weight and the number average molecular weight, as known in the art of polymer chemistry (see e.g. "Polymer Synthesis and Characterization", J.A. Nairn, University of Utah, 2003). The polydispersity index is a number which is greater than or equal to one, and it may be estimated from Gel Permeation Chromatographic data. When the polydispersity index is 1, the product is monodisperse and is thus made up of compounds with a single molecular weight. When the polydispersity index is greater than 1 it is a measure of the polydispersity of that polymer, i.e. how broad the distribution of polymers with different molecular weights is. The use of for example "mPEG20000" in formulas, compound names or in molecular structures indicates an mPEG residue wherein mPEG is polydisperse and has a molecular weight of approximately 20 kDa. The polydispersity index typically increases with the molecular weight of the PEG or mPEG. When reference is made to 20 kDa PEG and in particular 20 kDa mPEG it is intended to indicate a compound (or in fact a mixture of compounds) with a polydisperisty in- dex below 1.06, such as below 1.05, such as below 1.04, such as below 1.03, such as be-tween 1.02 and 1.03. When reference is made to 30 kDa PEG and in particular 30 kDa mPEG it is intended to indicate a compound (or in fact a mixture of compounds) with a polydisperisty index below 1.06, such as below 1.05, such as below 1.04, such as below 1.03, such as between 1.02 and 1.03. When reference is made to 40 kDa PEG and in particular 40 kDa mPEG it is intended to indicate a compound (or in fact a mixture of compounds) with a polydisperisty index below 1.06, such as below 1.05, such as below 1.04, such as below 1.03, such as between 1.02 and 1.03 In the present context, the words "peptide" and "protein" are used interchangeably and are intended to indicate the same. The term "peptide" is intended to indicate a compound with two or more amino acid residues linked by a peptide bond. The amino acids may be natural or unnatural. The term is also intended to include said compounds substituted with other peptides, saccharides, lipids, or other organic compound, as well as compounds wherein one or more amino acid residue have been chemically modified. The term is also intended to include peptides to which prosthetic groups are attached. In particular, the peptide exerts a physiological, such as e.g. a therapeutic activity. In the present context, the term "aryl" is intended to indicate a homocyclic aromatic ring radical or a fused homocyclic ring system radical wherein at least one of the rings are aromatic. Typical aryl groups include phenyl, biphenylyl, naphthyl, tetralinyl and the like. The term "heteroaryl", as used herein, alone or in combination, refers to an aromatic ring radical with for instance 5 to 7 ring atoms, or to a fused aromatic ring system radical with for instance from 7 to 18 ring atoms, wherein at least on ring is aromatic and contains one or more heteroatoms as ring atoms selected from nitrogen, oxygen, or sulfur heteroatoms, wherein N-oxides and sulfur monoxides and sulfur dioxides are permissible heteroaromatic substitutions. Examples include furanyl, thienyl, thiophenyl, pyrrolyl, imidazolyl, pyrazolyl, tri-azolyl, tetrazolyl, thiazolyl, oxazolyl, isoxazolyl, oxadiazolyl, thiadiazolyl, isothiazolyl, pyridinyl, pyridazinyl, pyrazinyl, pyrimidinyl, quinolinyl, isoquinolinyl, benzofuranyl, benzothio-phenyl, indolyl, and indazolyl, and the like. The term "conjugate" as a noun is intended to indicate a modified peptide, i.e. a peptide with a moiety bonded to it to modify the properties of said peptide. As a verb, the term is intended to indicate the process of bonding a moiety to a peptide to modify the properties of said peptide. The term "prodrug" as used herein is intended to indicate a compound which not or which not necessarily has a therapeutic activity but which upon administration is transformed into a therapeutically active compound by a reaction taking place in the body. Typically such reactions are hydrolysis, e.g. by esterases or oxidations. Examples of prodrugs include bio-hydrolyzable amides and biohydrolyzable esters and also encompasses a) compounds in which the biohydrolyzable functionality in such a prodrug is encompassed in the compound according to the present invention, and b) compounds which may be oxidized or reduced bio-logically at a given funcţional group to yield drug substances according to the present invention. Examples of these funcţional groups include 1,4-dihydropyridine, N-alkylcarbonyl-1,4-dihydropyridine, 1,4-cyclohexadiene, tert-butyl, and the like. As used herein, the term "biohydrolyzable ester" is an ester of a drug substance (in casu, a compound according to the invention) which either a) does not interfere with the bio-logical activity of the parent substance but confers on that substance advantageous proper-ties in vivo such as duration of action, onset of action, and the like, or b) is biologically inactive but is readily converted in vivo by the subject to the biologically active principie. The ad-vantage is, for example increased solubility or that the biohydrolyzable ester is orally ab-sorbed from the gut and is transformed to a compound according to the present invention in plasma. Many examples of such are known in the art and include by way of example lower alkyl esters (e.g., Ci-C4), lower acyloxyalkyl esters, lower alkoxyacyloxyalkyl esters, alkoxya-cyloxy esters, alkyl acylamino alkyl esters, and choline esters. As used herein, the term "biohydrolyzable amide" is an amide of a drug substance (in casu, a compound according to the present invention) which either a) does not interfera with the biologica! activity of the parent substance but confers on that substance advantageous properties in vivo such as duration of action, onset of action, and the like, or b) is biologically inactive but is readily converted in vivo by the subject to the biologically active principie. The advantage is, for example increased solubility or that the biohydrolyzable amide is orally absorbed from the gut and is transformed to a compound according to the present invention in plasma. Many examples of such are known in the art and include by way of example lower alkyl amides, a-amino acid amides, alkoxyacyl amides, and alkylaminoalkylcar-bonyl amides. In the present context, the term "pharmaceutically acceptable salt" is intended to indicate salts which are not harmful to the patient. Such salts include pharmaceutically acceptable acid addition salts, pharmaceutically acceptable metal salts, ammonium and alkylated ammonium salts. Acid addition salts include salts of inorganic acids as well as organic acids. Representative examples of suitable inorganic acids include hydrochloric, hydrobromic, hy-droiodic, phosphoric, sulfuric, nitric acids and the like. Representative examples of suitable organic acids include formic, acetic, trichloroacetic, trifluoroacetic, propionic, benzoic, cin-namic, citric, fumărie, glycolic, lactic, maleic, malic, malonic, mandelic, oxalic, picric, pyruvic, salicylic, succinic, methanesulfonic, ethanesulfonic, tartaric, ascorbic, pamoic, bismethylene salicylic, ethanedisulfonic, gluconic, citraconic, aspartic, stearic, palmitic, EDTA, glycolic, p-aminobenzoic, glutamic, benzenesulfonic, p-toluenesulfonic acids and the like. Further ex-amples of pharmaceutically acceptable inorganic or organic acid addition salts include the pharmaceutically acceptable salts listed in J. Pharm. Sci. 1977, 66, 2, which is incorporated herein by reference. Examples of metal salts include lithium, sodium, potassium, magnesium salts and the like. Examples of ammonium and alkylated ammonium salts include ammo-nium, methylammonium, dimethylammonium, trimethylammonium, ethylammonium, hy-droxyethylammonium, diethylammonium, butylammonium, tetramethylammonium salts and the like. A "therapeutically effective amount" of a compound as used herein means an amount sufficient to cure, alleviate or partially arrest the clinica! manifestations of a given disease and its complications. An amount adequate to accomplish this is defined as "therapeutically effective amount". Effective amounts for each purpose will depend on the severity of the disease or injury as well as the weight and general state of the subject. It will be un-derstood that determining an appropriate dosage may be achieved using routine experimen-tation, by constructing a matrix of values and testing different points in the matrix, which is all within the ordinary skills of a trained physician or veterinar/. The term "treatment" and "treating" as used herein means the management and care of a patient for the purpose of combating a condition, such as a disease or a disorder. The term is intended to include the full spectrum of treatments for a given condition from which the patient is suffering, such as administration of the active compound to alleviate the symptoms or complications, to delay the progression of the disease, disorder or condition, to alleviate or relief the symptoms and complications, and/or to cure or eliminate the disease, disorder or condition as well as to prevent the condition, wherein prevention is to be under-stood as the management and care of a patient for the purpose of combating the disease, condition, or disorder and includes the administration of the active compounds to prevent the onset of the symptoms or complications. The patient to be treated is preferably a mammal, in particular a human being, but it may also include animals, such as dogs, cats, cows, sheep and pigs. DESCRIPTION OF THE INVENTION Transglutaminase (E.C.2.3.2.13) is also known as protein-glutamine-y-glutamyltransferase and catalyses the general reaction (Formula Removed)In one embodiment, Q-C(O)-NH2 (amine acceptor) represents a glutamine containing peptide and Q'-NH2 (amine donor) then represents a first compound, as indicated above, or Q-C(O)-NH2 represents a first compound as indicated above and Q'-NH2 then represents a lysine containing peptide. In a particular embodiment, however, Q-C(O)-NH2 represents a glutamine containing peptide and Q'-NH2 represents a first compound as indicated above. A common amine donor in vivo is peptide bound lysine, and the above reaction then affords cross-bonding of peptides. The coagulation factor Factor XIII is a transglutaminase which effects clotting of blood upon injurios. Different transglutaminases differ from each other, e.g. in what amino acid residues around the Gin are required for the protein to be a substrate, i.e. different transglutaminases will have different GIn-containing peptides as sub-startes depending on what amino acid residues are neighbours to the Gin residue. This aspect can be exploited if a peptide to be modified contains more than one Gin residue. If it is desired to selectively conjugate the peptide only at some of the Gin residues present, this selectivity can be obtained be selection of a transglutaminase which only accepts the relevant Gin residue(s) as substrate. Alternatively, one or more amino acid residues close to a Gin may be altered, e.g. by means of genetic engineering to modify the activity of a given transglutaminase to said Gin residue. It is recognised that whether or not a compound is substrate for a given enzyme in principie depends on the reaction conditions, e.g. the time frame. Given sufficient time, many compounds not normally regarded as substrates are, in fact, substrates. When it is stated above that for a given transglutaminase some Gin residues may be substrates while other are not it is intended to indicate that "others are not" to an extend where the desired selectivity can still be achieved. If one or more Gin residues, which it is desired to leave unconju-gated, is, in fact, a substrate for transglutaminase, however, only if in contact with transglutaminase for an extended period of time, selectivity may be achieved by removing or inacti-vating the transglutaminase after a suitable time. Examples of useful transglutaminases include microbial transglutaminases, such as e.g. from Streptomyces mobaraense, Streptomyces cinnamoneum and Streptomyces griseo-carneum (a\\ disclosed in US 5,156,956, which is incorporated herein by reference), and Streptomyces lavendulae (disclosed in US 5,252,469, which is incorporated herein by reference) and Streptomyces ladakanum (JP2003199569, which is incorporated herein by reference). It should be noted that members of the former genus Streptoverticillium are now included in the genus Streptomyces [Kaempfer, J.Gen.Microbiol., 137, 1831-1892, 1991]. Other useful microbial transglutaminases have been isolated from Bacillus subtilis (disclosed in US 5,731,183, which is incorporated herein by reference) and from various Myxomycetes. Other examples of useful microbial transglutaminases are those disclosed in WO 96/06931 (e. g. transglutaminase from Bacilus lydicus) and WO 96/22366, both of which are incorporated herein by reference. Useful non-microbial transglutaminases include guinea-pig liver transglutaminase, and transglutaminases from various marine sources like the flat fish Pa-grus major (disclosed in EP-0555649, which is incorporated herein by reference), and the japanese oyster Crassostrea gigas (disclosed in US 5,736,356, which is incorporated herein by reference). In one embodiment, Q'-NH2, i. e. the first compound as indicated above, is a nitrogen containing nucleophile, wherein a nucleophile is understood to be a basic, electron-rich compound which tends to attack the nucleus of carbon. A nitrogen containing nucleophile can for instance be an amine or an oxy amine derivative. In one embodiment, the invention relates to a method of conjugating peptides, wherein a Gin residue containing peptide represented by the formula NH2 is reacted in one or mores steps with a nitrogen containing nucleophile (first compound) represented by the formula H2N-D-R-X in the presence of a transglutaminase to form a transaminated peptide of the formula (Formula Removed) optionally said latent funcţional group in X is then activated, said transaminated peptide being further reacted with a second compound of the formula Y-E-Z to form a conjugated peptide of the formula wherein D represents a bond or oxygen; R represents a linker or a bond; X represents a radical comprising one or more funcţional groups or latent funcţional groups not accessible in the amino acid residues constituting the peptide P-C(O)-NH2; Y represents a radical comprising one or more funcţional groups which groups react with funcţional groups present in X, and which funcţional groups do not react with funcţional groups accessible in the peptide P-C(0)-NH2; E represents a linker or a bond; A represents the moiety formed by the reaction between the pair of funcţional groups com- prised in X and Y; and Z is the moiety to be conjugated to the peptide. Following the conjugation, the conjugated peptide may be isolated and purified by techniques well-known in the art. The conjugated peptide may also be converted into a phar-maceutically acceptable salt or prodrug, if relevant. In particular, said method may also comprise a step wherein the resulting conjugated peptide is formulated as a pharmaceutical composition. The moiety A formed in the reaction between the funcţional groups of X and Y may in principie be of any kind depending on what properties of the final conjugated peptide is desired. In some situation it may be desirable to have a labile bond which can be cleaved at some later stage, e.g. by some enzymatic action or by photolysis. In other situations, it may be desirable to have a stable bond, so that a stable conjugated peptide is obtained. Particular mentioning is made of the type of moieties formed by reactions between amine deriva-tives and carbonyl groups, such as oxime, hydrazone, phenylhydrazone and semicarbazone moieties. In one embodiment the funcţional groups of X and Y are selected from amongst car bonyl groups, such as keto and aldehyde groups, and amino derivatives, such as hydrazine derivatives -NH-NH2, hydrazine carboxylate derivatives -O-C(0)-NH-NH2, semicarbazide derivatives -NH-C(O)-NH-NH2, thiosemicarbazide derivatives -NH-C(S)-NH-NH2, carbonic acid dihydrazide derivatives -NHC(0)-NH-NH-C(O)-NH-NH2, carbazide derivatives -NH-NH-C(O)-NH-NH2, thiocarbazide derivatives -NH-NH-C(S)-NH-NH2, aryl hydrazine derivatives -NH-C(O)-C6H4-NH-NH2, and hydrazide derivatives -C(O)-NH-NH2; or oxylamine derivatives, such as -O-NH2, -C(O)-O-NH2, -NH-C(0)-O-NH2 and -NH-C(S)-O-NH2. It is to be understood, that if the funcţional group comprised in X is a carbonyl group, then the funcţional group comprised in Y is an amine derivative, and vice versa. Due to the presence of-NH2 groups in most peptides, a better selectivity is believed to be obtained if X comprises a keto- or an aldehyde- functionality. Another example of a suitable pair of funcţional groups present in X and Y is azide derivatives (-N3) and alkynes which react to form a triazole moiety. Still another example of a suitable pair is alkyne and nitril-oxide which react to form a isooxazolidine moiety. It is to be understood that the funcţional group comprised in X may be latent^in the sense that it has to be activated prior to the reaction with Y-E-Z. By way of example, X may comprise a moiety which upon reaction with a suitable reagent is transformed to an aldehyde or a ketone. Examples of such moieties include (Figure Removed) wherein R9 represents H, d-ealkyl, aryl or heteroaryl. Particular examples include methyl, ethyl and propyl. Said moieties may be transformed to an aldehyde or ketone by oxidation with a suitable agent, such as e.g. periodate, or by hydrolysis with an aqueous acid, option-ally in the presence of a catalyst, such as copper, silver, or mercury salts. In particular, the compound of the formula (first compound), H2N-D-R—X may be selected from amongst 4-(aminomethyl)phenyl ethanone, 4-(2-aminoethyl)phenyl ethanone, N-(4-acetylphenyl) 2-aminoacetamide, 1-[4-(2-aminoethoxy)phenyl]ethanone, 1-[3-(2-aminoethoxy)phenyl]ethanone, 1,4-bis(aminoxy)butane, 3-oxapentane-1,5-dioxyamine, 1,8-diaminoxy-3,6-dioxaoctane, 1,3-bis(aminoxy)propan-2-ol, 1,11-bis(aminoxy)-3,6,9-trioxaundecane, 1,3-diamino-2-propanol, 1,2-bis(aminoxy)ethane, and 1,3-bis(aminoxy)propane. Both the compound to transaminate (first compound) and the compound to be re-acted with the transaminated peptide (second compound) comprises a linker, R and E, re-spectively. These linkers, which are independent of each other, may be absent or selected from amongst alkane, alkene or alkyne diradicals and hetero alkane, hetero alkene and het- ero alkyne diradicals, wherein one or more optionally substituted aromatic homocyclic biradi-cal or biradical of a heterocyclic compound, e.g. phenylene or piperidine biradical may be inserted into the aforementioned biradicals. It is to be understood that said linkers may also comprise substitutions by groups selected from amongst hydroxyl, halogen, nitro, cyano, carboxyl, aryl, alkyl and heteroaryl. Both E and R represent bonds or linkers, and in the present context the term "linker" is intended to indicate a moiety functioning as a means to separate Y from Z and X from NH2-D-, respectively. One function of the linkers E and R may be to provide adequate flexibil-ity in the linkage between the peptide and the conjugated moiety Z. Typical examples of E and R include straight, branched and/or cyclic Ci-i0alkylene, C2-ioalkenylene, C2_i0alkynylene, C2-i0heteroalkylene, C2.i0heteroalkenylene, C2.10heteroalkynylene, wherein one or more homocyclic aromatic compound biradical or heterocyclic compound biradical may be inserted. Particular examples of E and R include (Figure Removed) wherein * denotes points of attachment. A need for modifying peptides may arise for any number of reasons, and this is also reflected in the kinds of compounds that may be conjugated to peptides according to the methods of the present invention. It may be desirable to conjugate peptides to alter the phys-ico-chemical properties of the peptide, such as e.g. to increase (orto decrease) solubility to modify the bioavailability of therapeutic peptides. In another embodiment, it may be desirable to modify the clearance rate in the body by conjugating compounds to the peptide which binds to plasma proteins, such as e.g. albumin, or which increase the size of the peptide to prevent or delay discharge through the kidneys. Conjugation may also alter and in particular decrease the susceptibility of a peptide to hydrolysis, such as e.g. in vivo proteolysis. In another embodiment, it may be desirable to conjugate a labei to facilitate analysis of the peptide. Examples of such labei include radioactive isotopes, fluorescent markers and enzyme substrates. In still another embodiment, a compound is conjugated to a peptide to facilitate isolation of the peptide. For example, a compound with a specific affinity to a particular col-umn material may be conjugated to the peptide. It may also be desirable to modify the im-munogenecity of a peptide, e.g. by conjugating a peptide so as to hide, mask or eclipse one or more immunogenic epitopes at the peptide. In one embodiment, the invention provides a method of improving pharmacological properties of peptides. The improvement is with respect to the corresponding un-conjugated peptide. Examples of such pharmacological properties include funcţional in vivo half-life, im-munogencity, renal filtration, protease protection and albumin binding. The term "funcţional in vivo half-life" is used in its normal meaning, i.e., the time at which 50% of the biologica! activity of the peptide or conjugated peptide are still present in the body/target organ, or the time at which the activity of the peptide or conjugated peptide is 50% of its iniţial value. As an alternative to determining funcţional in vivo half-life, "in vivo plasma half-life" may be determined, i.e., the time at which 50% of the peptide or peptide conjugate circulate in the plasma or bloodstream prior to being cleared. Determination of plasma half-life is often more simple than determining funcţional half-life and the magnitude of plasma half-life is usually a good indication of the magnitude of funcţional in vivo half-life. Alternative terms to plasma half-life include serum half-life, circulating half-life, circulatory half-life, serum clearance, plasma clearance, and clearance half-life. The term "increased" as used in connection with the funcţional in vivo half-life or plasma half-life is used to indicate that the relevant half-life of the peptide conjugate is statis-tically significantly increased relative to that of the un-conjugated (parent) peptide, as determined under comparable conditions. For instance the relevant half-life may be increased by at least about 25%, such as by at lest about 50%, e.g., by at least about 100%, 150%, 200%, 250%, or 500%. In one embodiment, the compounds of the present invention exhibit an in-crease in half-life of at least about 5 h, preferably at least about 24 h, more preferably at least about 72 h, and most preferably at least about 7 days, relative to the half-life of the parent peptide. Measurement of in vivo plasma half-life can be carried out in a number of ways as described in the literaturo. An increase in in vivo plasma half-life may be quantified as a de-crease in clearance (CL) or as an increase in mean residence time (MRT). Conjugated peptides of the present invention for which the CL is decreased to less than 70%, such as less than 50%, such than less than 20%, such than less than 10% of the CL of the parent peptide as determined in a suitable assay is said to have an increased in vivo plasma half-life. Conjugated peptides of the present invention for which MRT is increased to more than 130%, such as more than 150%, such as more than 200%, such as more than 500% of the MRT of the parent peptide in a suitable assay is said to have an increased in vivo plasma half-life. Clearance and mean residence time can be assessed in standard pharmacokinetic studies using suitable test animals. It is within the capabilities of a person skilled in the art to choose a suitable test animal for a given protein. Tests in human, of course, represent the ultimate test. Typically, and as an example, the mice, rats, dogs, monkeys or pigs are in injected with the compiound of interest. The amount injected depends on the test animal. Subsequently, blood samples are taken over a period of one to five days as appropriate for the assessment of CL and MRT. The blood samples are conveniently analysed by ELISA techniques. The term "Immunogenicity" of a compound refers to the ability of the compound, when administered to a human, to elicit a deleterious immune response, whether humoral, cellular, or both. In any human sub-population, there may exist individuals who exhibit sensi-tivity to particular administered proteins. Immunogenicity may be measured by quantifying the presence of growth hormone antibodies and/or growth hormone responsive T-cells in a sensitive individual, using convenţional methods known in the art. In one embodiment, the conjugated peptide of the present invention exhibit a decrease in immunogenicity in a sensitive individual of at least about 10%, preferably at least about 25%, more preferably at least about 40% and most preferably at least about 50%, relative to the immunogenicity for that individual of the parent peptide. The term "protease protection" or "protease protected" as used herein is intended to indicate that the conjugated peptide of the present invention is more resistant to the plasma peptidase or proteases than is the parent peptide. Protease and peptidase enzymes present in plasma are known to be involved in the degradation of circulating proteins. Resistance of a protein to degradation by for instance dipeptidyl aminopeptidase IV (DPPIV) is determined by the following degradation assay: Aliquots of the protein (5 nmol) are incubated at 37 °C with 1 uL of purified dipeptidyl aminopeptidase IV corresponding to an enzymatic activity of 5 mU for 10-180 minutes in 100 uL of 0.1 M triethylamine-HCI buffer, pH 7.4. Enzymatic reactions are terminated by the addition of 5 uL of 10% trifluoroacetic acid, and the protein degradation products are separated and quantified using HPLC analysis. One method for performing this analysis is : The mixtures are applied onto a Vydac C18 widepore (30 nm pores, 5 um particles) 250 x 4.6 mm column and eluted at a flow rate of 1 ml/min with linear stepwise gradients of acetonitrile in 0.1% trifluoroacetic acid (0% acetoni-trile for 3 min, 0-24% acetonitrile for 17 min, 24-48% acetonitrile for 1 min) according to Siegel et al., Regul. Pept. 1999;79:93-102 and Mentlein et al. Eur. J. Biochem. 1993;214:829-35. Proteins and their degradation products may be monitored by their ab-sorbance at 220 nm (peptide bonds) or 280 nm (aromatic amino acids), and are quantified by integration of their peak areas related to those of standards. The rate of hydrolysis of a protein by dipeptidyl aminopeptidase IV is estimated at incubation times which result in less than 10% of the peptide being hydrolysed. In one embodiment, the rate of hydrolysis of the pep- tide conjugate is less than 70%, such as less than 40%, such as less than 10% of that of the parent peptide. The most abundant protein component in circulating blood of mammalian species is serum albumin, which is normally present at a concentration of approximately 3 to 4.5 grams per 100 millilitres of whole blood. Serum albumin is a blood protein of approximately 70,000 daltons which has several important functions in the circulatory system. It functions as a transportor of a variety of organic molecules found in the blood, as the main transportor of various metabolites such as fatty acids and bilirubin through the blood, and, owing to its abundance, as an osmotic regulator of the circulating blood. Serum albumin has a half-life of more than one week, and one approach to increasing the plasma half-life of proteins has been to conjugate to the protein a group that binds to serum albumin. Albumin binding prop-erty may be determined as described in J.Med.Chem, 43, 2000, 1986-1992, which is incor-porated herein by reference. Particular examples of Z include radicals comprising one or more labels, such as fluorescent markers, such as fluorescein radical, rhodamine radical, Texas Red ® radical and phycobili protein radical; enzyme substrates, such as p-nitrophenol acetate radical; and radioactive isotopes, such as Cu-64, Ga67, Ga-68, Zr-89, Ru-97, Tc-99, Rh-105, Pd-109, In-111,1-123,1-125,1-131, Re-186, Re-188, Au-198, Pb-203, At-211, Pb-212 and Bi-212; organic moieties, such as PEG or mPEG radicals and amino derivatives thereof (including straight and branched PEG and mPEG radicals); straight, branched and/or cyclic C^alkyl, C2-22alkenyl, C2-22alkynyl, Ci^heteroalkyl, C2.22heteroalkenyl, C2-22heteroalkynyl, wherein one or more homocyclic aromatic compound biradical or heterocyclic compound biradical may be inserted, and wherein said CrC22 or C2-C22 radicals may optionally be substituted with one or more substituents selected from hydroxyl, halogen, carboxyl, heteroaryl and aryl, wherein said aryl or heteroaryl may optionally be further substituted by one or more substituents selected from hydroxyl, halogen, and carboxyl; steroid radicals; lipid radicals; polysaccharide radicals, e.g. dextrans; polyamide radicals e.g. polyamino acid radicals; PVP radicals; PVA radicals; poly(1-3-dioxalane); poly(1,3,6-trioxane); ethylene/maleic anhydride polymer; Ci-bacron dye stuffs, such as Cibacron Blue 3GA; polyamide chains of specified length, as dis-closed in WO 00/12587, which is incorporated herein by reference; and hydroxyalkyl starch, such as e.g. hydroxyethyl starch, such as disclosed in WO 03/074087 and WO 02/80979, both of which are incorporated herein by reference. Particular mentioning is made of Cio.2oalkyl, such as C15 and d7, and in particular linear Ci5 and Ci7, and benzophenone derivatives of the formula Particular mentioning is made of Z comprising a cibacronyl radical as sketched be- Low (Figure Removed) The PEG or mPEG conjugated to a peptide according to the present invention may be of any molecular weight. In particular the molecular weight may be between 500 and 1000,000 Da, such as between 500 and 500,000 Da, such as between 500 and 100,000 Da, such as between 500 and 60,000 Da, such as between 1000 and 40,000 Da, such as between 5000 and 40,000 Da. In particular, PEG with molecular weights of between 10,000 Da and 40,000 Da, such as between 20,000 Da and 40,000 Da, such as between 20,000 and 30,000 Da or between 30,000 and 40,000 Da may be used. Particular mentioning is made of PEG or mPEG with a molecular weight of 10,000, 20,000, 30,000 or 40,000 Da. Z may be branched so that Z comprises more than one of the above mentioned la-bels or radicals. For instance, mPEG40K is typically achieved as a branched mPEG with two arm each comprising a mPEG20k. In one embodiment, Z comprises one or more moieties that are known to bind to plasma proteins, such as e.g. albumin. The ability of a compound to bind to albumin may be determined as described in J.Med.Chem, 43, 2000, 1986-1992, which is incorporated herein by reference. In the present context, a compound is defined as binding to albumin if Ru/Da is above 0.05, such as above 0.10, such as above 0.12 or even above 0.15. In another embodiment of the invention the albumin binding moiety is a peptide, such as a peptide comprising less than 40 amino acid residues. A number of small peptides which are albumin binding moieties are disclosed in J. Biol Chem. 277, 38 (2002) 35035-35043, which is incorporated herein by reference. Particular examples of compounds of the formula Y-E-Z include (Figure Removed) wherein each k in the above formulas independently represent an integerfrom O to 5, i.e. O, 1,2, 3, 4 or 5. As discussed in the "Background of the invention" part, direct conjugation of e.g. amine functionalised PEG orfatty acids to Gin containing peptides is known. It is, however, clearfrom the examples disclosed in, e.g. EP 950665, EP 785276, Sato, Adv. Drug Delivery Rev., 54, 459-476, 2002 and Wada, Biotech. Lett., 23, 1367-1372, 2001 that it requires a significant excess (up to 100-1000 fold) of the compound to be conjugated to the peptide for the reaction to proceed. Such excess constituie a limitation to the utility of the reaction in technical or large scale. For instance, mPEG with a small poly dispersity index are very ex-pensive, and a requirement for a large excess is in practise prohibitive. Moreover, for the conjugation of large moieties, such as e.g. PEG 10 kDa or PEG 20k Da, excess of the re-agent in the order of 100-1000 fold is not feasible due to the molecular weight of such com-pounds. It is also well-known that the presence of large amounts of PEG is likely to precipitate peptides, i.e. both the peptide to be conjugated and the transglutaminase. In contrast hereto, the present two-step method offers the advantage that the reactant which in the en- zymatic step is required in large excess is a small molecule which can easily be handled even in large excess. With a proper selection of the bond to be formed in the second step no large excess is required as e.g. oxime formation takes place at almost equimolar amounts of amine- and keto-functionalities. A further advantage is the possibility to make "ready-to-conjugate" peptides. A peptide may be reacted with a suitable nucleophile (H2N-D-R-X) in the presence of a transgluta-minase to generate a functionalised peptide. Said functionalised peptide may then be stored as needed to be reacted later with one or more second compound (Y-E-Z) to generate vari-ous different conjugated peptides. This allows one functionalised peptide to be used to generate a multitude of conjugated peptides. In this way, numerous optimisations to identify ap-propriate reaction conditions can be avoided. A peptide has to be a substrate for transglutaminase according to the methods of the present invention. It is thus a requirement that the peptide contains a Gin or a Lys residue, and in particular a Gin residue. If a given peptide is not a transglutaminase substrate it is possible to insert one or more Gin or Lys residues, and in particular Gin residues in the peptide sequence to make the peptide a substrate for transglutaminase. In principie , such Gin or Lys residue may be inserted at any position in the sequence, however, it is preferably in-serted at a position where the physiological, such as the therapeutic activity of the peptide is not affected to a degree where the peptide is not useful anymore, e.g. in a therapeutic inter-vention. Insertions of amino acid residues in peptides can be brought about by standard techniques known to persons skilled in the art, such as post-translational chemical modifica-tion or transgenetic techniques. Any peptide which are substrates to transglutaminase can be conjugated by the methods of the present invention, such as e.g. enzymes, peptide hormones, growth factors, antibodies, cytokines, receptors, lymphokines and vaccine antigenes, and particular mention-ing is made of therapeutic peptides, such as insulin, glucagon like-peptide 1 (GLP-1), gluca-gon like-peptide 2 (GLP-2), growth hormone, cytokines, trefoil factor peptides (TFF), peptide melanocortin receptor modifiers and factor VII compounds. Particular applicable insulin is human insulin. In the present context the term "human insulin" refers to naturally produced insulin or recombinantly produced insulin. Recombinant human insulin may be produced in any suitable host cel l, for example the nost cells may be bacteria!, fungal (including yeast), insect, animal or plant cells. Many insulin compounds have been disclosed in the literature, and they too are particular useful in the methods of the present invention. By "insulin compound" (and related expressions) is meant human insulin in which one or more amino acids have been deleted and/or replaced by other amino acids, including non-codeable amino acids, and/or human insulin comprising additional amino ac-ids, i.e. more than 51 amino acids, and/or human insulin in which at least one organic sub-stituent is bound to one or more of the amino acids. The following patent documents are mentioned as disclosures of insulin compounds particularly applicable in the methods provided by the present invention. WO 97/31022 (Novo Nordisk), which is incorporated herein by reference, discloses insulin compounds with a protracted activity profile wherein the amino group of the N-terminal amino acid of the B-chain and/or the e-amino group of Lys829 nas a carboxylic acid containg lipophilic substituent. Particular mentioning is made of NeB29-(CO-(CH2)i4-COOH) human insulin; NeB29-(CO-(CH2)i6-COOH) human insulin; NEB29-(CO-(CH2)i8-COOH) human insulin; NeB29-(CO-(CH2)20-COOH); NEB29-(CO-(CH2)22-COOH) human insulin; NeB29-(CO-(CH2)14-COOH) Asp828 -human insulin; NeB29-(CO-(CH2)16-COOH) Asp828 -human insulin; NEB29-(CO-(CH2)18-COOH) Asp828 -human insulin; NEB29-(CO-(CH2)20-COOH) Asp628 -human insulin; NeB29-(CO-(CH2)22-COOH) Asp828 -human insulin; N6B30-(CO-(CH2)14-COOH) Thr^Lys^-human insulin; NeB30-(CO-(CH2)16-COOH) Thr^Lys^-human insulin; NeB30-(CO-(CH2)18-COOH) Thr^Lys^-human insulin; NeB30-(CO-(CH2)20-COOH) Thr^Lys^-human insulin; NeB30-(CO-(CH2)22-COOH) ThrB29LysB30-human insulin; N6B28-(CO-(CH2)i4-COOH) LysB28ProB29-human insulin; NeB28-(CO-(CH2)16-COOH) LysB28ProB29-human insulin; N6B28-(CO-(CH2)18-COOH) LysB28ProB29-human insulin; NeB28-(CO-(CH2)20-COOH) LysB28ProB29-human insulin; NeB28-(CO-(CH2)22-COOH) LysB28ProB29-human insulin; NEB29-(CO-(CH2)14-COOH) desB30 human insulin; NeB29-(CO-(CH2)i6-COOH) desB30 human insulin; NeB29-(CO-(CH2)18-COOH) desBSO human insulin; N6B29-(CO-(CH2)20-COOH) desBSO human insulin; and NeB29-(CO-(CH2)22COOH) desB30 human insulin. WO 96/29344 (Novo Nordisk), which is incoporated herein by reference, discloses insulin compounds with a protracted activity profile wherein either the amino group of the N-terminal amino acid of the B-chain has a lipophilic substituent comprising from 12 to 40 carbon atoms attached, or wherein the carboxylic acid group of the C-terminal amino acid of the B-chain has a lipophilic substituent comprising from 12 to 40 carbon atoms attached. WO 95/07931 (Novo Nordisk), which is incorporated herein by reference, discloses insulin compounds with a protracted activity profile, wherein the e-amino group of Lys629 has a lipophilic substituent. Particular mentioning is made of NEB29-tridecanoyl des(B30) human insulin, NEB29-tetradecanoyl des(BSO) human insulin, NeB29-decanoyl des(BSO) human insulin, NEB29-dodecanoyl des(BSO) human insulin, NEB29-tridecanoyl Gl/21 des(BSO) human insulin, NEB29-tetradecanoyl Gl/21 des(BSO) human insulin, NEB29-decanoyl Gl/21 des(B30) human insulin, NeB29-dodecanoyl Gly*21 des(B30) human insulin, NeB29-tridecanoyl Gly*21 Gin63 des(B30) human insulin, NEB29-tetradecanoyl Gly*21 Gin63 des(B30) human insulin, NeB29-decanoyl Gly*21 Gin83 des(B30) human insulin, NEB29-dodecanoyl Gly*21 Gin83 des(B30) human insulin, NeB29-tridecanoyl Ala*21 des(B30) human insulin, NeB29-tetradecanoyl Ala*21 des(BSO) human insulin, NeB29-decanoyl Ala*21 des(BSO) human insulin, NeB29-dodecanoyl AlaA21 des(BSO) human insulin, NeB29-tridecanoyl Ala*21 Gin83 des(B30) human insulin, NeB29-tetradecanoyl Ala*21 Gin83 des(B30) human insulin, NeB29-decanoyl Ala*21 Gin83 des(B30) human insulin, Ne829-dodecanoyl Ala*21 Gin83 des(BSO) human insulin, NE829-tridecanoyl Gin83 des(BSO) human insulin, NeB29-tetradecanoyl Gin83 des(B30) human insulin, Ne829-decanoyl Gin83 des(B30) human insulin, NEB29-dodecanoyl Gin83 des(B30) human insulin, NEB29-tridecanoyl Gly*21 human insulin, NeB29-tetradecanoyl Gly*21 human insulin, NEB29-decanoyl Gly*21 human insulin, NEB29-dodecanoyl Gly*21 human insulin, NEB29-tridecanoyl Gly*21 Gin83 human insulin, NEB29-tetradecanoyl Gly*21 Gin83 human insulin, NeB29-decanoyl Gly*21 Gin83 human insulin, NEB29-dodecanoyl Gly*21 Gin83 human insulin, NeB29-tridecanoyl Ala*21 human insulin, Ne829-tetradecanoyl Ala*21 human insulin, NeB29-decanoyl Ala*21 human insulin, NE829-dodecanoyl Ala*21 human insulin, NEB29-tridecanoyl Ala*21 Gin63 human insulin, NeB29-tetradecanoyl Ala*21 Gin83 human insulin, NeB29-decanoyl Ala*21 Gin83 human insulin, NEB29-dodecanoyl Ala*21 Gin83 human insulin, NEB29-tridecanoyl Gin83 human insulin, NeB29-tetradecanoyl Gin83 human insulin, NEB29-decanoyl Gin83 human insulin, NEB29-dodecanoyl Gin83 human insulin, NE829-tridecanoyl Glu830 human insulin, NE829-tetradecanoyl Glu830 human insulin, NeB29-decanoyl GluB3° human insulin, Ne829-dodecanoyl Glu830 human insulin, NEB29-tridecanoyl Gly*21 Glu830 human insulin, NEB29-tetradecanoyl Gly*21 Glu630 human insulin, NeB29-decanoyl Gly*21 Glu830 human insulin, NEB29-dodecanoyl Gly*21 Glu830 human insulin, NEB29-tridecanoyl Gly*21 Gin83 Glu830 human insulin, NeB29-tetradecanoyl Gly*21 Gin83 Glu830 human insulin, NeB29-decanoyl Gly*21 Gin83 Glu830 human insulin, NeB29-dodecanoyl Gly*21 Gin83 Glu830 human insulin, NeB29-tridecanoyl Ala*21 Glu830 human insulin, NeB29-tetradecanoyl Ala*21 Glu830 human insulin, NeB29-decanoyl Ala*21 Glu830 human insulin, NeB29-dodecanoyl Ala*21 Glu830 human insulin, NeB29-tridecanoyl Ala*21 Gin83 Glu830 human insulin, NEB29-tetradecanoyl Ala*21 Gin83 Glu830 human insulin, NeB29-decanoyl Ala*21 Gin83 Glu830 human insulin, NEB29-dodecanoyl Ala*21 Gin83 Glu830 human insulin, NeB29-tridecanoyl Gin83 Glu830 human insulin, NeB29-tetradecanoyl Gin83 Glu830 human insulin, NeB29-decanoyl Gin83 Glu830 human insulin and N6829-dodecanoyl Gin83 Glu830 human insulin. WO 97/02043 (Novo Nordisk), which is incorporated herein by reference discloses hormonally inactive insulin compounds which are useful in insulin prophylaxis, and in particular such analogues of human insulin are selected from amongst desA1 human insulin; des(A1-A2) human insulin; des(A1-A3) human insulin; desA21 human insulin; des(B1-B5) human insulin; des(B1-B6) human insulin; des(B23-B30) human insulin; des(B24-B30) human insulin; des(B25-B30) human insulin; Gly^ human insulin; AlaA2 human insulin; Nle^ human insulin; Thr*2 human insulin; Pro*2 human insulin; D-alIo Ile*2 human insulin; Nva*3 human insulin; NleA3 human insulin; LeuA3 human insulin; Val^.lle*3 human insulin; AbuA2,AbuA3 human insulin; Gly^.Gly*3 human insulin; D-CysA6 human insulin; D-CysA6,D-CysA11 human insulin; SerA6,SerA11,des(A8-A10) human insulin; D-CysA7 human insulin; D-CysA11 human insulin; LeuA19 human insulin; Gly86 human insulin; Glu812 human insulin; Asn812 human insulin; Phe812 human insulin; D-Ala812 human insulin; and Asp825 human insulin are applicable in the methods of the present invention. WO 92/15611 (Novo nordisk), which is incorporated herein by reference, discloses analogues of human insulin with a fast association rate constants in the insulin receptor binding process and characterised by comprising a tyrosine in position A13 and/or a phenylalanin, tryptophane ortyrosine in position B17. In particular, such analogues are selected from amongst Tyr"^ human insulin, PheB" human insulin, TrpB" human insulin, TyrB^7 human insulin, Tyr™ ,pneB17 human insulin, Tyr" ,jrpB17 numan jnsulin, Tyr^ ,TyrB17 human insulin, PheA13,PheB17 human insulin, PheA13,Trp^''7 human insulin, PheA13,TyrB17 human insulin, TrpA13,pheB17 human insulin, TrpA^,Trp^7 human insulin and TrpA^3,Tyr B17 human insulin. WO 92/00322 (Novo Nordisk), which is incorporated herein by reference, discloses analogues of human insulin which are capable of being targeted to specific tissues, and which are characterized by having in the A13 position and/or in the B17 position in the insulin molecule a naturally occurring amino acid residue different from leucine and/or by having in the B18 position in the insulin molecule a naturally occurring amino acid residue different from valine. In particular, such analogues are selected from amongst AlaB^7 human insulin, AlaB^ human insulin, AsnA13 human insulin, AsnA13,AlaB17human insulin, AsnA13,Asp^^7 human insulin, AsnA13,GluB17 human insulin, AsnB1^ human insulin, AspA^3 human insulin, AspA13 ,AlaB17 human insulin, AspA13,AspB^7 human insulin, AspA^,Glu^7 human insulin, AspB^ human insulin, GlnA^ human insulin, GlnA1^,AlaB17 human insulin, GlnA^,AspB17 human insulin, GlnB^ human insulin, GluA^ human insulin, GluA^,AlaB17 human insulin, GluA^ ,AspB17 human insulin, GluA13,GluB^7 human insulin, GluB^ human insulin, GlyA13 human insulin, GlyA13,AlaB17 human insulin, GlyA13,AsnB17 human insulin, GlyA13,AspB17 human insulin, GlyA^3,GluB17 human insulin, GlyB^8 human insulin, Ser^3 human insulin, Ser^13 ,GlnA17,GluB10,GlnB17-des(ThrB3°) human insulin, SeA^.AIa817 human insulin, SeA13 ,AsnB17 human insulin, Ser^.Asp617 human insulin, SerA^.GIn617 human insulin, SeA13 ,GluB17 human insulin, SeA^.Thr817 human insulin, SerB14,AspB17 human insulin, Ser618 human insulin, Thr^13 human insulin orThr818 human insulin. WO 90/01038 (Novo Nordisk), which is incorporated herein by reference, discloses analogues of human insulin with high biologica! activity and characterized by having Phe825 substituted by His or Tyr, by having substitutions in one or more of positions A4, A8, A17, A21, B9, B10, B12, B13, B21, B26, B27, B28 and B30, and by having the amino acid residue at position B30 optionally absent. In particular, such analogues are selected from amongst Tyr825 human insulin, Tyr^.Asp828 human insulin, His625 human insulin, HisB25,AspB2B human insulin, Tyr825 human insulin -B30-amide and His825 human insulin-B30-amide. WO 86/05496 (Nordisk Gentofte) discloses analogues of human insulin with a protracted action and characterized by having a blocked B30 carboxylic group, and by having one to four blocked carboxylic groups in the amino acid residues at positions A4, A17, A21, B13 and B21. In particular, such analogues are selected from amongst insulin-B30-octyl ester, insulin-B30-dodecyl amide, insulin-B30-hexadecyl amide, insulin-(B21,B30)-dimethyl ester, insulin-(B17,B30)-dimethyl ester, insulin-(A4,B30) diamide, insulin-A17amide-B30-octyl ester, insulin-(A4,B13)-diamide-B30-hexylamide, insulin-(A4,A17,621 ,B30)-tetraamide, insulin-(A17,B30)-diamide, A4-Ala-insulin-B30-amide and B30-Leu-insulin-(A4,B30)-diamide. WO 86/05497(Nordisk Gentofte), which is incorporated herein by reference, discloses insulin compounds in which one or more of the four amino acid residues in positions A4, A17, B13 and B21 comprises an uncharged side chain. Particular mentioning is made of human insulin A17-Gln, human insulin A4-Gln, porcine insulin B21-Gln, human insulin B13-Gln, human insulin (A17,621 )-Gln, human insulin A4-Ala, human insulin B21-Thr, human insulin 613-Val, human insulin-Thr-A17-Gln, human insulin B21-methyl ester and human insulin A17-methyl ester. WO 92/00321 (Novo Nordisk), which is incorporated herein by reference, discloses insulin compounds with prolonged activity wherein a positive charge in the N-terminal end of the 8-chain has been introduced. Particular mentioning is made of Arg .SeA ,Thr B30-NH2 human insulin, ArgB5,ProB6,SerA21,ThrB30-NH2 human insulin, ArgB5,GlyA21,Thr B30-NH2 human insulin, ArgB5,ProB6,GlyA21,ThrB30-NH2 human insulin, ArgB2,SerA21,Thr B30-NH2 human insulin, ArgB2,ProB3,SerA21,ThrB30-NH2 human insulin, ArgB2,GlyA21 ,Thr B30-NH2 human insulin, ArgB2,ProB3,GlyA21,ThrB30-NH2 human insulin, ArgB2,ArgB3,Ser A21 ,ThrB30-NH2 human insulin, ArgB2,ArgB3,SerA21 human insulin, ArgB4,ProB5,SerA21 ,Thr B30-NH2 human insulin, ArgB4,ArgB5,ProB6,GlyA21 Jhr630 human insulin, ArgB3,GlyA21 ,Thr B30-NH2 human insulin, ArgB3,SerA21,ThrB30-NH2 human insulin, ArgB4,GlyA21,ThrB30-NH 2 human insulin, ArgB4,SerA21,ThrB30-NH2 human insulin and ArgB1,ProB2,GlyA21,ThrB3°-NH2 human insulin. WO 90/07522 (Novo Nordisk), which is incorporated herein by reference, dis-closes insulin compounds exhibiting a low ability to associate in solution wherein there is a posi-tively charged amino acid residue, i.e. Lys or Arg in the position B28. Particular mentioning is made of des[PheB25]-human insulin, desfTy^-human insulin, desllhr^l-human insulin, des[ProB28]-human insulin, des[PheB25]-porcine insulin, des[Pro828]-porcine insulin, des[Pro828]-rabbit insulin, des[PheB25],des[ThrB30]-human insulin, desITyr^.destThO-human insulin, [SeO-despro^-human insulin, [Gl/^-despro^-human insulin, [Gly^j-destPhe825]-human insulin, [AspA21]-des[PheB25]-human insulin, [HisB25]-des[Tyi£2%des[ThrB30]-human insulin, [AsnB25]-des[TyrB26],des[ThrB30]-human insulin, [Asp^desphe^.deslJhr^-human insulin, [AspB28]-des[PheB25]-human insulin, [Asp^-desphe^J-human insulin, [LysB28]-human insulin, [Lys^.Thr^-human insulin and [ArgB28]-des[LysB29]-human insulin. WO 90/11290 (Novo Nordisk), which is incorporated herein by reference dis-closes insulin compounds with a prolonged activity. Particular mentioning is made of [ArgA0]-human insulin-(B30-amide), [ArgAO,GlnB13]-human insulin-(B30-amide), [ArgAO,GlnA4,AspA21]-human insulin-(B30-amide), [Arg^.SeO-human insulin-(B30-amide) and [ArgAO,ArgB27]-desprh^J-human insulin. WO 90/10645 (Novo Nordisk), which is incorpotated herein by reference dis-closes glycosylated insulins. Particular mentioning is made of Phe(B1) glucose human insulin, Phe(B1) mannose human insulin, Gly(A1) mannose human insulin, Lys(B29) mannose human insulin, Phe(B1) galactose human insulin, Gly(A1) galactose human insulin, Lys(B29) galactose human insulin, Phe(B1) maltose human insulin, Phe(B1) lactose human insulin, Gly(A1) glucose human insulin, Gly(A1) maltose human insulin, Gly(A1) lactose human insulin, Lys(B29) glucose human insulin, Lys(B29) maltose human insulin, Lys(B29) lactose human insulin, Gly(A1),Phe(B1) diglucose human insulin, Gly(A1 ),Lys(B29) diglucose human insulin, Phe(B1),Lys(B29) diglucose human insulin, Phe(B1) isomaltose human insulin, Gly(A1) isomal- tose human insulin, Lys(B29) isomaltose human insulin, Phe(B1) maltotriose human insulin, Gly(A1) maltotriose human insulin, Lys(B29) maltotriose human insulin, Gly(A1),Phe(B1) dimal-tose human insulin, Gly(A1),Lys(B29) dimaltose human insulin, Phe(B1),Lys(B29) dimaltose human insulin, Gly(A1),Phe(B1) dilactose human insulin, Gly(A1 ),Lys(B29) dilactose human insulin, Phe(B1),Lys(B29) dilactose human insulin, Gly(A1),Phe(B1) dimaltotriose human insulin, Gly(A1),Lys(B29) dimaltotriose human insulin, Phe(B1),Lys(B29) dimaltotriose human insulin, Phe(B1),Gly(A1) dimannose human insulin, Phe(B1 ),Lys(B29) dimannose human insulin, Gly(A1),Lys(B29) dimannose human insulin, Phe(B1),Gly(A1) digalactose human insulin, Phe(B1),Lys(B29) digalactose human insulin, Gly(A1 ),Lys(B29) digalactose human insulin, Phe(B1),Gly(A1) diisomaltose human insulin, Phe(B1),Lys(B29) diisomaltose human insulin, Gly(A1 ),Lys(B29) diisomaltose human insulin, Phe(B1) glucose [AspB1°] human insulin and Gly(A1),Phe(B1) diglucose [AspB1°] human insulin. WO 88/065999 (Novo Nordisk), which is incorporated herein by reference, dis-closes stabilized insulin compounds, wherein Ans21A has been substituted with other amino acid residues. Particular mentioning is made of Gly"2^ human insulin, Ala"2^ human insulin, Ser ^21 human insulin, Thc^l human insulin and hSer^21 human insulin. EP 254516 (Novo Nordisk), which is incorporated herein by reference, discloses insulin compounds with a prolonged action, wherein basic amino acid residues have been substituted by neutral amino acid residues. Particular mentioning is made of GlyA21,Ly8B27,ThrB30-NH2 human insulin, Ser^.Lys627 ,ThrB30-NH2 human insulin, ThrA21,LysB27,ThrB30-NH2 human insulin, AlaB21,LysB27,ThrB30-NH2 human insulin, HisA21,LysB27,ThrB30-NH2 human insulin, AspB21lLysB27lThrfl30-NN2 human Insulin, GlyA21,ArgB21,ThrB30-NH2 human insulin, Ser*21 ,ArgB27, Thr630- NH2 human insulin, ThrA21,ArgB27,ThrB3°- NH2 human insulin, AlaB21,ArgB27,ThrB30-NH2 human insulin, HisA21,ArgB27,ThrB3°- NH2 human insulin, Asp^.Arg^.Thr630- NH2 human insulin, GlnB13,GlyA21,ArgB27,ThrB30-NH2 human insulin, GlnB13!SerA21,ThrB30-NH2 human insulin, GlnB13,SerA21,ArgB27,ThrB30-NH2 human insulin, GlnB13,ThrA21,ArgB27,ThrB30-NH2 human insulin, GlnB13,AlaA21,ArgB27,ThrB30-NH2 human insulin, GlnB13,HisA21,ArgB27,ThrB30-NH2 human insulin, GlnB13,AspA21,ArgB27,ThrB30-NH2 human insulin, GlnB13,GlyA21,LysB27,ThrB30-NH2 human insulin, GlnB13,SerA21,LysB27,ThrB30-NH2 human insulin, GlnB13,ThrA21,LysB27,ThrB30-NH2 human insulin, GlnB13,AlaA21,LysB27,ThrB30-NH2 human insulin, GlnB13,HisA21,LysB27,ThrB30-NH2 human insulin, GlnB13,AspA21,LysB27,ThrB30-NH2 human insulin, Asn^.Lys627 human insulin, Ser^.Lys627 hu-man insulin, Thr^.Lys627 human insulin, Ala^.Lys827 human insulin, His^.Lys827 human insulin, AspA21,LysB27 human insulin, GlyA21,LysB27 human insulin, AsnA21,ArgB27 human insulin, SerA21,ArgB27 human insulin, ThrA21,ArgB27 human insulin, AlaA21,ArgB27 human insulin, HisA21,ArgB27 human insulin, AspA21,ArgB27 human insulin, GlyA21,Arg827 human insulin, GlnA17,Asn*21,ArgB27human insulin, GlnA17,SerA21,ArgB27human insulin, GlnA17,ThrA21,ArgB27human insulin, GlnA17,AlaA21,ArgB27human insulin, GlnA17,HisA21,ArgB27human insulin, GlnA17,AspA21,ArgB27human insulin, GlnA17,GlyA21,ArgB27human insulin, GlnA17,AsnA21,GlnB13human insulin, GlnA17,SerA21,GlnB13human insulin, GlnA17,Thr^1,GlnB13human insulin, GlnA17,AlaA21,GlnB13human insulin, GlnA17,HisA21,GlnB13human insulin, GlnA17,AspA21,GlnB13human insulin, Gln^.Gly^.GIn^human insulin, ArgA27,AsnA21,GlnB13human insulin, ArgA27,SerA21,GlnB13human insulin, ArgA27,ThrA21,GlnB13human insulin, Arg^.Ala^.GIn^human insulin, ArgA27,HisA21,GlnB13human insulin, Arg^.Asp^.GIn^human insulin, ArgA27,GlyA21,GlnB13human insulin, GlnA17,AsnA21,LysB27human insulin, Gln^.Ser^Lys^human insulin, GlnA17,ThrA21,LysB27human insulin, GlnA17,AlaA21,LysB27human insulin, GlnA17,HisA21,LysB27human insulin, GlnA17,AspA21,LysB27human insulin, GlnA17,GlyA21,LysB27human insulin, GlnB13,AsnA21,LysB27human insulin, GlnB13,SerA21,LysB27human insulin, GlnB13,ThrA21,LysB27human insulin, GlnB13,AlaA21,LysB27human insulin, GlnB13,HisA21,LysB27human insulin, GlnB13,AspA21,LysB27human insulin, and GlnB13,GlyA21,LysB27human insulin. EP 214826 (Novo Nordisk), which is incorporated herein by reference, discloses rapid onset insulin compounds. EP 194864 (Novo Nordisk), which is incorporated herein by reference, discloses insulin compounds with a prolonged action, wherein basic amino acid residues have been substituted by neutral amino acid residues. Particular mentioning is made of GlnA17,ArgB27,ThrB30-NH2 human insulin, GlnA17,GlnB13,ThrB30-NH2 human insulin, GlnA17,LysB27,ThrB30-NH2 human insulin, GlnA17,LysB27-NH2 human insulin, GlnA17, GlnA17,ThrB30-NH2 human insulin, GlnB13,ArgB27,ThrB30-NH2 human insulin, GlnB13,LysB27,ThrB30-NH2 human insulin, GlnB13,LysB30-NH2 human insulin, GlnB13,ThrB30-NH2 human insulin, ArgB27,ArgB3°- NH2 human insulin, ArgB27,LysB3°- NH2 human insulin, ArgB27,ThrB3°- NH2 human insulin, LysB27,ArgB3°- NH2 human insulin, LysB27,LysB3°- NH2 human insulin, Lys^.Thr830- NH2 human insulin, LysB29-NH2,des-(B30)human insulin, Thr630-NH2 human insulin, LysB3°- NH2 human insulin, LysB30(Lau)- NH2 human insulin, LysB30,ArgB31- NH2 human insulin, LysB30,LysB31- NH2 human insulin, ArgB3°- NH2 human insulin, ArgB30,ArgB31- NH2 human insulin, and ArgB30,LysB31- NH2 human insulin. US Patent No. 3,528,960 (Eli Lilly), which is incorporated herein by reference, discloses N-carboxyaroyl insulin compounds in which one, two orthree primary amino groups of the insulin molecule nas a carboxyaroyl group. GB Patent No. 1.492.997 (Nat. Res. Dev. Corp.), which is incorporated herein by reference, discloses insulin compounds with a carbamyl substitution at NsB29 with an improved profile of hypoglycaemic effect. JP laid-open patent application No. 1-254699 (Kodama Co., Ltd.), which is incorporated herein by reference, discloses insulin compounds, wherein an alkanoyl group is bound to the amino group of PheB1 or to the e-amino group of Lys829 or to both of these.. JP laid-open patent application No. 57-067548 (Shionogi), which is incorporated herein by reference discloses insulin compounds, in which the B30 position nave an amino acid having at least five carbon atoms which cannot necessarily be coded for by a triplet of nucleo-tides. WO 03/053339 (Eli Lilly), which is incorporated herein by reference, disclose insulin compounds, wherein the A-chain in the N-terminal has been extended with two amino acid residues, A-1 and AO, wherein the B-chain has been extended at the N-terminal with two amino acid residues, B-1 and BO, wherein the amino acid residues at positions B28, B29 and B39 may be substituted, and wherein the e-amino group of Lys at position B28 or B29 is covalently bound to the a-carboxyl group of a positively charged amino acid to form a Lys-Ne-aminoacid derivative. Particular mentioning is made of said analogues, wherein A-1 and B-1 are both absent, and wherein AO represent Arg and BO represents Arg or is absent. Insulin compounds selected from the group consisting of i.An analogue wherein position B28 is Asp, Lys, Leu, Val, or Ala and position B29 is Lys or Pro; and ii.des(B28-B30), des(B27) or des(BSO) human insulin. are also applicable for the methods of the present invention, and in particular, the insulin compound wherein position B28 is Asp or Lys, and position B29 is Lys or Pro. des(B30) human insulin is also applicable in the methods of the present invention. Other applicable insulin compounds are selected from the group consisting of B29-N6-myristoyl-des(B30) human insulin, B29-NE-palmitoyl-des(B30) human insulin, B29-NE-myristoyl human insulin, B29-N6-palmitoyl human insulin, B28-N6-myristoyl Lys628 Pro829 human insulin, B28-NE-palmitoyl Lys828 Pro829 human insulin, BSO-N'-myristoyl-Thr^Lys830 human insulin, BSO-N'-palmitoyl-Th^Lys630 human insulin, B29-NE-(N-palmitoyl-Y-glutamyl)-des(B30) human insulin, B29-N6-(N-lithocholyl-y-glutamyl)-des(B30) human insulin, B29-NE- (co-carboxyheptadecanoyl)-des(B30) human insulin, B29-Ne-(<»-carboxyheptadecanoyl) hu-man insulin and B29-Ne-myristoyl-des(B30) human insulin. Examples of GLP-1 applicable in the methods of the present invention include human GLP-1 and GLP-1 compounds. Human GLP-1 is a 37 amino acid residue peptide originating from preproglucagon which is synthesised i.a. in the L-cells in the distal ileum, in the pancreas and in the brain. GLP-1 is an important gut hormone with regulatory function in glucose metabolism and gastrointestinal secretion and metabolism. Processing of preproglucagon to give GLP-1 (7-36)-amide, GLP-1 (7-37) and GLP-2 occurs mainly in the L-cells. The frag-ments GLP-1 (7-36)-amide and GLP-1 (7-37) are both glucose-dependent insulinotropic agents. In the past decades a number of structural analogues of GLP-1 were isolated from the venom of the Gila monster lizards (Heloderma suspectum and Heloderma horridum). Exendin-4 is a 39 amino acid residue peptide isolated from the venom of Heloderma horridum, and this peptide shares 52% homology with GLP-1. Exendin-4 is a potent GLP-1 receptor agonist which has been shown to stimulate insulin release and ensuring lowering of the blood glucose level when injected into dogs. The group of GLP-1 (1-37) and exendin-4(1-39) and certain fragments, analogues and derivatives thereof (designated GLP-1 compounds herein) are potent insulinotropic agents, and they are all applicable in the method of the present invention. Insulinotropic fragments of GLP-1(1-37) are insulinotropic peptides for which the entire sequence can be found in the sequence of GLP-1 (1-37) and where at least one terminal amino acid has been deleted. Examples of insulinotropic fragments of GLP-1 (1-37) are GLP-1(7-37) wherein the amino acid residues in positions 1-6 of GLP-1(1-37) have been deleted, and GLP-1 (7-36) where the amino acid residues in position 1-6 and 37 of GLP-1 (1-37) have been deleted. Examples of insulinotropic fragments of exendin-4(1-39) are exendin-4(1-38) and exendin-4(1-31). The insulinotropic property of a compound may be determined by in vivo or in vitro assays well known in the art. For instance, the compound may be admin-istered to an animal and monitoring the insulin concentration overtime. Insulinotropic ana-logs of GLP-1(1-37) and exendin-4(1-39) refer to the respective molecules wherein one or more of the amino acids residues have been exchanged with other amino acid residues and/or from which one or more amino acid residues have been deleted and/or from which one or more amino acid residues have been added with the proviso that said analogue either is insulinotropic or is a prodrug of an insulinotropic compound . Examples of insulinotropic analogs of GLP-1 (1-37) is e.g. Met8-GLP-1(7-37) wherein the alanine in position 8 has been replaced by methionine and the amino acid residues in position 1 to 6 have been deleted, and Arg34-GLP-1(7-37) wherein the valine in position 34 has been replaced with arginine and the amino acid residues in position 1 to 6 have been deleted. An example of an insulinotropic analog of exendin-4(1-39) is Ser2Asp3-exendin-4( 1-39) wherein the amino acid residues in position 2 and 3 have been replaced with serine and aspartic acid, respectively (this particular analog also being known in the art as exendin-3). Insulinotropic derivatives of GLP-1(1-37), exendin-4(1-39) and analogs thereof are what the person skilled in the art considers to be derivatives of these peptides, i.e. having at least one substituent which is not present in the parent peptide molecule with the proviso that said derivative either is insulinotropic or is a prodrug of an insulinotropic compound. Examples of substituents are amides, carbohydrates, alkyl groups and lipophilic substituents. Examples of insulinotropic derivatives of GLP-1(1-37), exendin-4(1-39) and analogs thereof are GLP-1(7-36)-amide, Arg34, Lys26(N£-(y-Glu(Na-hexadecanoyl)))-GLP-1(7-37) and Tyr^-exendin^l-SIJ-amide. Further examples of GLP-1(1-37), exendin-4(1-39), insulinotropic fragments thereof, insulinotropic analogs thereof and insulinotropic derivatives thereof are described in WO 98/08871, WO 99/43706, US 5424286 and WO 00/09666, which are all enclosed herein by reference. GLP-2 and GLP-2 compounds may also be modified by the methods provided by the present invention. In the present context a GLP-2 compound binds to a GLP-2 receptor, preferably with an affinity constant (KD) or a potency (EC50) of below 1 uM, e.g. below 100 nM. The term "GLP-2 compound" is intended to indicate human GLP-2 in which one or more amino acid residue has been deleted and/or replaced by another amino acid residue, natural or unnatural, and/or human GLP-2 comprising additional amino acid residues, and/or human GLP-2 in which at least one organic substituent is bound to one or more of the amino acid residues. In particular, those peptides are considered, which amino acid sequence exhibit at any sequence of 33 consecutive amino acids more than 60% of the amino acid sequence of human GLP-2. Also those peptides are considered, which amino acid sequence exhibit at any sequence of 37 consecutive amino acids more than 60% of the amino acid sequence of human GLP-2 when up to four amino acids are deleted from the amino acid sequence. Also those peptides are considered, which amino acid sequence exhibit at any sequence of 31 consecutive amino acids more than 60% of the amino acid sequence of GLP-2, when up to two amino acids are added to their amino acid sequence. The term "GLP compounds" also includes natural allelic variations that may exist and occur from one individual to another. Also, degree and location of glycosylation or other post-translation modifications may vary depending on the chosen host cells and the nature of the host cellular environment. Candidate GLP-2 compounds, which may be used according to the present invention include the GLP-2 compounds described in WO 96/32414, WO 97/39031, WO 98/03547, WO 96/29342, WO 97/31943, WO 98/08872, which are all incorporated herein by reference. In particular, the following GLP-2 compounds are applicable in the methods of the present invention. A2G-GLP-2(1-33); K30R-GLP-2(1-33); S5K-GLP-2(1-33); S7K-GLP-2(1-33); D8K-GLP-2(1-33); E9K-GLP-2(1-33); M10K-GLP-2(1-33); N11K-GLP-2(1-33); T12K-GLP-2(1-33); H3K-GLP-2(1-33); L14K-GLP-2(1-33); D15K-GLP-2(1-33); N16K-GLP-2(1-33); L17K-GLP-2(1-33); A18K-GLP-2(1-33); D21K-GLP-2(1-33); N24K-GLP-2(1-33); Q28K-GLP-2(1-33); S5K/K30R-GLP-2(1-33); S7K/K30R-GLP-2(1-33); D8K/K30R-GLP-2(1-33); E9K/K30R-GLP-2(1-33); M10K/K30R-GLP-2(1-33); N11K/K30R-GLP-2(1-33); T12K/K30R-GLP-2(1-33); M3K/K30R-GLP-2(1-33); L14K/K30R-GLP-2(1-33); D15K/K30R-GLP-2(1-33); N16K/K30R-GLP-2(1-33); L17K/K30R-GLP-2(1-33); A18K/K30R-GLP-2(1-33); D21K/K30R-GLP-2(1-33); N24K/K30R-GLP-2(1-33); Q28K/K30R-GLP-2(1-33); K30R/D33K-GLP-2(1-33); D3E/K30R/D33E-GLP-2(1 -33); D3E/S5K/K30R/D33E-GLP-2(1 -33); D3E/S7K/K30R/D33E-GLP-2(1-33);D3E/D8K/K30R/D33E-GLP-2(1-33);D3E/E9K/K30R/D33E-GLP-2(1-33); D3E/M10K/K30R/D33E-GLP-2( 1 -33); D3E/N11 K/K30R/D33E-GLP-2(1 -33); D3E/T12K/K30R/D33E-GLP-2(1 -33); D3E/113K/K30R/D33E-GLP-2(1 -33); D3E/L14K/K30R/D33E-GLP-2(1 -33); D3E/D15K/K30R/D33E-GLP-2(1 -33); D3E/N16K/K30R/D33E-GLP-2(1-33);D3E/L17K/K30R/D33E-GLP-2(1-33); D3E/A18K/K30R/D33E-GLP-2(1-33);D3E/D21K/K30R/D33E-GLP-2(1-33); D3E/N24K/K30R/D33E-GLP-2(1-33);andD3E/Q28K/K30R/D33E-GLP-2(1-33). GLP-2 derivatives with only one lipophilic substituent attached to the GLP-2 peptide are also applicable in the methods of the present invention, such as GLP-2 derivatives whe-rein the lipophilic substituent comprises from 4 to 40 carbon atoms, such as from 8 to 25 carbon atoms, e.g. from 12 to 20 carbon atoms. The lipophilic substituent may be attached to an amino acid residue in such a way that a carboxyl group of the lipophilic substituent forms an amide bond with an amino group of the amino acid residue. By way of example, the lipophilic substituent is attached to a Lys residue. The lipophilic substituent may be attached to an amino acid residue in such a way that an amino group of the lipophilic substituent forms an amide bond with a carboxyl group of the amino acid residue. The lipophilic substituent may also be attached to the GLP-2 peptide by means of a spacer, and said spacer may be selected from amongst p-alanine, gamma-aminobutyric acid (GABA), y-glutamic acid, Lys, Asp, Glu, a dipeptide containing Asp, a dipeptide containing Glu, or a dipeptide containing Lys. In one embodiment of the invention the spacer is p-alanine. A carboxyl group of the parent GLP-2 peptide may also form an amide bond with an amino group of a spacer, and the carboxyl group of the amino acid or dipeptide spacer forms an amide bond with an amino group of the lipophilic substituent. An amino group of the parent GLP-2 peptide may also form an amide bond with a carboxylic group of a spacer, and an amino group of the spacer forms an amide bond with a carboxyl group of the lipophilic substituent. In one embodiment of the invention the lipophilic substituent is a straight-chain or branched alkyl group. In one embodiment of the invention the lipophilic substituent is the acyl group of a straight-chain or branched fatty acid. In one embodiment of the invention the lipophilic substituent is an acyl group of a straight-chain or branched alkane a,co-dicarboxylic acid. In one embodiment of the invention the GLP-2 derivative has one lipophilic substituent. In one embodiment of the invention the GLP-2 derivative has two lipophilic substituents. In one embodiment of the invention the GLP-2 derivative has three lipophilic substituents. In one embodiment of the invention the GLP-2 derivative has four lipophilic substituents. The following list contains GLP-2 derivatives which are particular applicable in the methods of the present invention. S5K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); S7K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); D8K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); E9K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); M10K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); N11K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); T12K(3-(hexadecanoylamino)propionyl)-GLP-2(1 -33); H3K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); L14K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); D15K(3-(hexadecanoylamino)propionyl)-GLP-2(1 -33); N16K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); L17K(3-(octanoylamino)propionyl)-GLP-2(1-33); L17K(3-(nonanoylamino)propionyl)-GLP-2(1-33); L17K(3-(decanoylamino)propionyl)-GLP-2(1-33); L17K(3-(undecanoylamino)propionyl)-GLP-2(1 -33); L17K(3-(dodecanoylamino)propionyl)-GLP-2(1-33); L17K(3-(tridecanoylamino)propionyl)-GLP-2(1-33); L17K(3-(tetradecanoylamino)propionyl)-GLP-2(1 -33); L17K(3-(pentadecanoylamino)propionyl)-GLP-2(1-33) L17K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); L17K(3-(heptadecanoylamino)propionyl)-GLP-2(1 -33); L17K(3-(octadecanoylamino)propionyl)-GLP-2(1-33); L17K(3-(nonadecanoylamino)propionyl)-GLP-2(1-33); L17K(3-(eicosanoylamino)propionyl)-GLP-2(1 -33); L17K((S)-4-carboxy-4-(octanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(nonanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(decanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(undecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(dodecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(tridecanoylamino)butanoyl)-GLP-2(1 -33); L17K((S)-4-carboxy-4-(tetradecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(pentadecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(hexadecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(heptadecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(octadecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(nonadecanoylamino)butanoyl)-GLP-2(1-33); L17K((S)-4-carboxy-4-(eicosanoylamino)butanoyl)-GLP-2(1 -33); L17K(4-(octanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(nonanoylamino)butanoyl)-GLP-2(1 -33); L17K(4-(decanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(undecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(dodecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(tridecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(tetradecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(pentadecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(hexadecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(heptadecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(octadecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(nonadecanoylamino)butanoyl)-GLP-2(1-33); L17K(4-(eicosanoylamino)butanoyl)-GLP-2(1-33); A18K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); D21 K(3-(hexadecanoylamino)propionyl)-GLP-2(1 -33); N24K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); Q28K(3-(hexadecanoylamino)propionyl)-GLP-2(1-33); S5K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); S7K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); D8K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); E9K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); M10K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); N11 K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1 -33); T12K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1 -33); M3K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); L14K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); D15K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); N16K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(octanoylamino)propionyl)/K30R-GLP-2(1 -33); L17K(3-(nonanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(decanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(undecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(dodecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(tridecanoylamino)propionyl)/K30R-GLP-2( 1 -33); L17K(3-(tetradecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(pentadecanoylamino)propionyl)/K30R-GLP-2(1 -33); L17K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(heptadecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(octadecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(nonadecanoylamino)propionyl)/K30R-GLP-2(1-33); L17K(3-(eicosanoylamino)propionyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(octanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(nonanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(decanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(undecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(dodecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(tridecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(tetradecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(pentadecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(hexadecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(heptadecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(octadecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(nonadecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K((S)-4-carboxy-4-(eicosanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(octanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(nonanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(decanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(undecanoylamino)butanoyl)/K30R-GLP-2(1 -33); L17K(4-(dodecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(tridecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(tetradecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(pentadecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(hexadecanoylamino)butanoyl)/K30R-GLP-2(1 -33); L17K(4-(heptadecanoylamino)butanoyl)/K30R-GLP-2(1 -33); L17K(4-(octadecanoylamino)butanoyl)/K30R-GLP-2(1 -33); L17K(4-(nonadecanoylamino)butanoyl)/K30R-GLP-2(1-33); L17K(4-(eicosanoylamino)butanoyl)/K30R-GLP-2(1-33); A18K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); D21 K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1 -33); N24K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); Q28K(3-(hexadecanoylamino)propionyl)/K30R-GLP-2(1-33); D3E/S5K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/S7K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/D8K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/E9K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/M10K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/N11 K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1 -33); D3E/T12K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/l13K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L14K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/D15K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/N16K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(octanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(nonanoylamino)propionyl)/K30R/D33E-GLP-2(1 -33); D3E/L17K(3-(decanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(undecanoylamino)propionyl)/K30R/D33E-GLP-2(1 -33); D3E/L17K(3-(dodecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(tridecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(tetradecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(pentadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(heptadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(octadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(nonadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(3-(eicosanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(octanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(nonanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(decanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(undecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(dodecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(tridecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(tetradecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(pentadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(hexadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(heptadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(octadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(nonadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K((S)-4-carboxy-4-(eicosanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(octanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(nonanoylamino)butanoyl)/K30R/D33E-GLP-2(1 -33); D3E/L17K(4-(decanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(undecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(dodecanoylamino)butanoyl)/K30R/D33E-GLP-2(1 -33); D3E/L17K(4-(tridecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(tetradecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(pentadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(hexadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(heptadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(octadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(nonadecanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/L17K(4-(eicosanoylamino)butanoyl)/K30R/D33E-GLP-2(1-33); D3E/A18K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/D21K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33); D3E/N24K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33);and D3E/Q28K(3-(hexadecanoylamino)propionyl)/K30R/D33E-GLP-2(1-33). Factor VII compounds applicable in the methods of the present invention encom-passes wild-type Factor VII (i.e., a polypeptide having the amino acid sequence disclosed in U.S. Patent No. 4,784,950), as well as variants of Factor VII exhibiting substantially the same or improved biological activity relative to wild-type Factor VII, Factor Vll-related polypeptides as well as Factor VII derivatives and Factor VII conjugates. The term "Factor VII compounds" is intended to encompass Factor VII polypeptides in their uncleaved (zymogen) form, as well as those that nave been proteolytically processed to yield their respective bioactive forms, which may be designated Factor Vila. Typically, Factor VII is cleaved between residues 152 and 153 to yield Factor Vila. Such variants of Factor VII may exhibit different properties relative to human Factor VII, including stability, phospholipid binding, altered specific activity, and the like. As used herein, "Factor Vll-related polypeptides" encompasses polypeptides, including variants, in which the Factor Vila biological activity has been substantially modified or re-duced relative to the activity of wild-type Factor Vila. These polypeptides include, without limitation, Factor VII or Factor Vila into which specific amino acid sequence alterations have been introduced that modify or disrupt the bioactivity of the polypeptide. The term "Factor VII derivative" as used herein, is intended to designate wild-type Factor VII, variants of Factor VII exhibiting substantially the same or improved biological activity relative to wild-type Factor VII and Factor Vll-related polypeptides, in which one or more of the amino acids of the parent peptide have been chemically modified, e.g. by alkylation, PEGylation, acylation, ester formation or amide formation or the like. This includes but are not limited to PEGylated human Factor Vila, cysteine-PEGylated human Factor Vila and variants thereof. The term "PEGylated human Factor Vila" means human Factor Vila, having a PEG mole-cule conjugated to a human Factor Vila polypeptide. It is to be understood, that the PEG molecule may be attached to any part of the Factor Vila polypeptide including any amino acid residue or carbohydrate moiety of the Factor Vila polypeptide. The term "cysteine-PEGylated human Factor Vila " means Factor Vila having a PEG molecule conjugated to a sulfhydryl group of a cysteine introduced in human Factor Vila. The biological activity of Factor Vila in blood clotting derives from its ability to (i) bind to tissue factor (TF) and (ii) catalyze the proteolytic cleavage of Factor IX or Factor X to produce activated Factor IX or X (Factor IXa or Xa, respectively). For purposes of the invention, Factor Vila biological activity may be quantified by measuring the ability of a preparation to promote blood clotting using Factor VIl-deficient plasma and thromboplastin, as described, e.g., in U.S. Patent No. 5,997,864. In this assay, biological activity is expressed as the re-duction in clotting time relative to a control sample and is converted to "Factor VII units" by comparison with a pooled human serum standard containing 1 unit/ml Factor VII activity. Al-ternatively, Factor Vila biological activity may be quantified by (i) measuring the ability of Factor Vila to produce of Factor Xa in a system comprising TF embedded in a lipid membrane and Factor X. (Persson etal., J. Biol. Chem. 272:19919-19924, 1997); (ii) measuring Factor X hydrolysis in an aqueous system; (iii) measuring its physical binding to TF using an instrument based on surface plasmon resonance (Persson, FEBS Letts. 413:359-363, 1997) and (iv) measuring hydrolysis of a synthetic substrate. Factor VII variants having substantially the same or improved biological activity relative to wild-type Factor Vila encompass those that exhibit at least about 25%, preferably at least about 50%, more preferably at least about 75% and most preferably at least about 90% of the specific activity of Factor Vila that has been produced in the same cell type, when tested in one or more of a clotting assay, proteolysis assay, or TF binding assay as described above. Factor VII variants having substantially reduced biological activity relative to wild-type Factor Vila are those that exhibit less than about 25%, preferably less than about 10%, more preferably less than about 5% and most preferably less than about 1% of the specific activity of wild-type Factor Vila that has been produced in the same cell type when tested in one or more of a clotting assay, proteolysis assay, or TF binding assay as described above. Factor VII variants having a substantially modified biological activity relative to wild-type Factor VII include, without limitation, Factor VII variants that exhibit TF-independent Factor X proteolytic activity and those that bind TF but do not cleave Factor X. Variants of Factor VII, whether exhibiting substantially the same or better bioactivity than wild-type Factor VII, or, alternatively, exhibiting substantially modified or reduced bioactivity relative to wild-type Factor VII, include, without limitation, polypeptides having an amino acid sequence that differs from the sequence of wild-type Factor VII by insertion, deletion, or substitution of one or more amino acids. The terms "variant" or "variants", as used herein, is intended to designate Factor VII having the sequence of wild-type factor VII, wherein one or more amino acids of the parent protein nave been substituted by another amino acid and/or wherein one or more amino acids of the parent protein have been deleted and/or wherein one or more amino acids have been inserted in protein and/or wherein one or more amino acids have been added to the parent protein. Such addition can take place either at the N-terminal end or at the C-terminal end of the parent protein or both. The "variant" or "variants" within this definition still have FVII activity in its activated form. In one embodiment a variant is 70 % identical with the se-quence of wild-type Factor VII. In one embodiment a variant is 80 % identical with the se-quence of wild-type factor VII. In another embodiment a variant is 90 % identical with the se-quence of wild-type factor VII. In a further embodiment a variant is 95 % identical with the sequence of wild-type factor VII. Non-limiting examples of Factor VII variants having substantially the same biological activity as wild-type Factor VII include S52A-FVIIa, S60A-FVIIa ( Lino et al., Arch. Biochem. Biophys. 352: 182-192, 1998); FVIIa variants exhibiting increased proteolytic stability as dis-closed in U.S. Patent No. 5,580,560; Factor Vila that has been proteolytically cleaved be-tween residues 290 and 291 or between residues 315 and 316 (Mollerup et al., Biotechnol. Bioeng. 48:501-505,1995); oxidized forms of Factor Vila (Kornfelt et al., Arch. Biochem. Biophys. 363:43-54,1999); FVII variants as disclosed in PCT/DK02/00189; and FVII variants exhibiting increased proteolytic stability as disclosed in WO 02/38162 (Scripps Research Institute); FVII variants having a modified Gla-domain and exhibiting an enhanced membrane binding as disclosed in WO 99/20767 (University of Minnesota); and FVII variants as disclosed in WO 01/58935 (Maxygen ApS), all of which are incorporated herein by reference. Particular mentioning is made of FVII variants having increased biological activity compared to wild-type FVIIa include FVII variants as disclosed in WO 01/83725, WO 02/22776, WO 02/077218, PCT/DK02/00635, Danish patent application PA 2002 01423, Da-nish patent application PA 2001 01627; WO 02/38162 (Scripps Research Institute); and FVIIa variants with enhanced activity as disclosed in JP 2001061479 (Chemo-Sero-Therapeutic Res Inst.), all of which are incorporated herein by reference, all of which are incorporated herein by reference. Examples of Factor VII variants having substantially reduced or modified biological activity relative to wild-type Factor VII include R152E-FVIIa (Wildgoose et al., Biochem 29:3413-3420,1990), S344A-FVIIa (Kazama et al., J. Biol. Chem. 270:66-72, 1995), FFR-FVIIa (Holst et al., Eur. J. Vase. Endovasc. Surg. 15:515-520, 1998), and Factor Vila lacking the Gla do-main, (Nicolaisen et al., FEBS Letts. 317:245-249, 1993), all of which are incorporated herein by reference. Examples of variants of factor VII, factor VII or factor Vll-related polypeptides include wild-type Factor VII, L305V-FVII, L305V/M306D/D309S-FVII, L305I-FVII, L305T-FVII, F374P-FVII, V158T/M298Q-FVII, V158D/E296V/M298Q-FVII, K337A-FVII, M298Q-FVII, V158D/M298Q-FVII, L305V/K337A-FVII, V158D/E296V/M298Q/L305V-FVII, V158D/E296 V/M298Q/K337A-FVI l, V158D/E296V/M298Q/L305V/K337A-FVI l, K157A-FVI l, E296V-FVII, E296V/M298Q-FVII, V158D/E296V-FVII, V158D/M298K-FVII, and S336G-FVII, L305V/K337A-FVII, L305VA/158D-FVII, L305V/E296V-FVII, L305V/M298Q-FVII, L305VA/158T-FVII, L305V/K337A/V158T-FVII, L305V/K337A/M298Q-FVII, L305V/K337A/E296V-FVIl, L305V/K337AA/158D-FVIl, L305V/V158D/M298Q-FVI l, L305V/V158D/E296V-FVII, L305V/V158T/M298Q-FVII, L305VA/158T/E296V-FVII, L305V/E296V/M298Q-FVII, L305VA/158D/E296V/M298Q-FVII, L305V/V158T/E296V/M298Q-FVII,L305VA/158T/K337A/M298Q-FVII, L305VA/158T/E296V/K337A-FVII,L305VA/158D/K337A/M298Q-FVII, L305V/V158D/E296V/K337A-FVII, L305V/V158D/E296V/M298Q/K337A-FVII, L305V/V158T/E296V/M298Q/K337A-FVII,S314E/K316H-FVII, S314E/K316Q-FVII, S314E/L305V-FVII, S314E/K337A-FVII, S314E/V158D-FVII, S314E/E296V-FVII, S314E/M298Q-FVII, S314E/V158T-FVII, K316H/L305V-FVII, K316H/K337A-FVII, K316H/V158D-FVII, K316H/E296V-FVII, K316H/M298Q-FVII, K316HA/158T-FVM, K316Q/L305V-FVII, K316Q/K337A-FVII, K316QA/158D-FVII, K316Q/E296V-FVII, K316Q/M298Q-FVII, K316QA/158T-FVII, S314E/L305V/K337A-FVII, S314E/L305VA/158D-FVII, S314E/L305V/E296V-FVII, S314E/L305V/M298Q-FVII, S314E/L305VA/158T-FVII, S314E/L305V/K337AA/158T-FVII.S314E/L305V/K337A/M298Q-FVII, S314E/L305V/K337A/E296V-FVII,S314E/L305V/K337A/V158D-FVII, S314E/L305V/V158D/M298Q-FVII, S314E/L305V/V158D/E296V-FVII, S314E/L305VA/158T/M298Q-FVII,S314E/L305VA/158T/E296V-FVII, S314E/L305V/E296V/M298Q-FVII, S314E/L305VA/158D/E296V/M298Q-FVII, S314E/L305V/V158T/E296V/M298Q-FVII, S314E/L305V/V158T/K337A/M298Q-FVII, S314E/L305VA/158T/E296V/K337A-FVII.S314E/L305V/V158D/K337A/M298Q-FVII, S314E/L305V/V158D/E296V/K337A-FVII,S314E/L305VA/158D/E296V/M298Q/K337A-FVII, S314E/L305VA/158T/E296V/M298Q/K337A-FVII, K316H/L305V/K337A-FVII, K316H/L305VA/158D-FVIl, K316H/L305V/E296V-FVIl, «316H/L305V/M298Q-FVIl, K316H/L305VA/158T-FVII, K316H/L305V/K337A/V158T-FVII, K316H/L305V/K337A/M298Q-FVII, K316H/L305V/K337A/E296V-FVII, K316H/L305V/K337AA/158D-FVII, K316H/L305VA/158D/M298Q-FVII,K316H/L305V/V158D/E296V-FVII, K316H/L305VA/158T/M298Q-FVII, K316H/L305VA/158T/E296V-FVII, K316H/L305V/E296V/M298Q-FVII, K316H/L305VA/158D/E296V/M298Q-FVII, K316H/L305VA/158T/E296V/M298Q-FVII, K316H/L305VA/158T/K337A/M298Q-FVII, K316H/L305VA/158T/E296V/K337A-FVII, K316H/L305V/V158D/K337A/M298Q-FVII, K316H/L305VA/158D/E296V/K337A-FVII, K316H/L305VA/158D/E296V/M298Q/K337A-FVII, K316H/L305VA/158T/E296V/M298Q/K337A-FVII, K316Q/L305V/K337A-FVII K316Q/L305V/V158D-FVIl, K316Q/L305V/E296V-FVI l, K316Q/L305V/M298Q-FVIl, K316Q/L305VA/158T-FVII,K316Q/L305V/K337AA/158T-FVII,K316Q/L305V/K337A/M298Q-FVII, K316Q/L305V/K337A/E296V-FVII, K316Q/L305V/K337AA/158D-FVII, K316Q/L305VA/158D/M298Q-FVIl, K316Q/L305VA/158D/E296V-FVI l, K316Q/L305V/V158T/M298Q-FVI l, K316Q/L305V/V158T/E296V-FVI l, K316Q/L305V/E296V/M298Q-FVII, K316Q/L305VA/158D/E296V/M298Q-FVII, K316Q/L305VA/158T/E296V/M298Q-FVIl, K316Q/L305VA/158T/K337A/M298Q-FVIl, K316Q/L305V/V158T/E296V/K337A-FVII, K316Q/L305VA/158D/K337A/M298Q-FVII, K316Q/L305VA/158D/E296V/K337A-FVII, K316Q/L305V/V158D/E296V/M298Q/K337A-FVII, K316Q/L305V/V158T/E296V/M298Q/K337A-FVII, F374Y/K337A-FVII, F374Y/V158D-FVII, F374Y/E296V-FVII, F374Y/M298Q-FVII, F374YA/158T-FVII, F374Y/S314E-FVII, F374Y/L305V-FVII, F374Y/L305V/K337A-FVII, F374Y/L305VA/158D-FVII, F374Y/L305V/E296V-FVII, F374Y/L305V/M298Q-FVII, F374Y/L305VA/158T-FVII, F374Y/L305V/S314E-FVII, F374Y/K337A/S314E-FVII, F374Y/K337AA/158T-FVII, F374Y/K337A/M298Q-FVII, F374Y/K337A/E296V-FVII, F374Y/K337AA/158D-FVII, F374YA/158D/S314E-FVI l, F374YA/158D/M298Q-FVI l, F374YA/158D/E296V-FVI l, F374YA/158T/S314E-FVI l, F374YA/158T/M298Q-FVI l, F374Y/V158T/E296V-FVI l, F374Y/E296V/S314E-FVII, F374Y/S314E/M298Q-FVII, F374Y/E296V/M298Q-FVII, F374Y/L305V/K337AA/158D-FVII, F374Y/L305V/K337A/E296V-FVII, F374Y/L305V/K337A/M298Q-FVII, F374Y/L305V/K337AA/158T-FVII, F374Y/L305V/K337A/S314E-FVII, F374Y/L305VA/158D/E296V-FVII, F374Y/L305VA/158D/M298Q-FVII, F374Y/L305VA/158D/S314E-FVII, F374Y/L305V/E296V/M298Q-FVII, F374Y/L305V/E296VA/158T-FVII, F374Y/L305V/E296V/S314E-FVII, F374Y/L305V/M298QA/158T-FVII, F374Y/L305V/M298Q/S314E-FVII, F374Y/L305VA/158T/S314E-FVII, F374Y/K337A/S314EA/158T-FVII, F374Y/K337A/S314E/M298Q-FVII, F374Y/K337A/S314E/E296V-FVII, F374Y/K337A/S314EA/158D-FVII, F374Y/K337AA/158T/M298Q-FVII, F374Y/K337AA/158T/E296V-FVII, F374Y/K337A/M298Q/E296V-FVII, F374Y/K337A/M298QA/158D-FVII, F374Y/K337A/E296VA/158D-FVI l, F374Y/V158D/S314E/M298Q-FVI l, F374YA/158D/S314E/E296V-FVII, F374YA/158D/M298Q/E296V-FVII, F374YA/158T/S314E/E296V-FVII, F374YA/158T/S314E/M298Q-FVII, F374YA/158T/M298Q/E296V-FVII, F374Y/E296V/S314E/M298Q-FVII, F374Y/L305V/M298Q/K337A/S314E-FVII, F374Y/L305V/E296V/K337A/S314E-FVII, F374Y/E296V/M298Q/K337A/S314E-FVII, F374Y/L305V/E296V/M298Q/K337A-FVII, F374Y/L305V/E296V/M298Q/S314E-FVII, F374YA/158D/E296V/M298Q/K337A-FVII, F374YA/158D/E296V/M298Q/S314E-FVII,F374Y/L305V/V158D/K337A/S314E-FVII, F374YA/158D/M298Q/K337A/S314E-FVII, F374YA/158D/E296V/K337A/S314E-FVII, F374Y/L305VA/158D/E296V/M298Q-FVII, F374Y/L305V/V158D/M298Q/K337A-FVII, F374Y/L305VA/158D/E296V/K337A-FVI l, F374Y/L305VA/158D/M298Q/S314E-FVI l, F374Y/L305VA/158D/E296V/S314E-FVII, F374YA/158T/E296V/M298Q/K337A-FVII, F374YA/158T/E296V/M298Q/S314E-FVII, F374Y/L305VA/158T/K337A/S314E-FVII, F374YA/158T/M298Q/K337A/S314E-FVII, F374YA/158T/E296V/K337A/S314E-FVII, F374Y/L305VA/158T/E296V/M298Q-FVII, F374Y/L305VA/158T/M298Q/K337A-FVII, F374Y/L305VA/158T/E296V/K337A-FVII, F374Y/L305VA/158T/M298Q/S314E-FVII, F374Y/L305VA/158T/E296V/S314E-FVII, F374Y/E296V/M298Q/K337AA/158T/S314E-FVII, F374YA/158D/E296V/M298Q/K337A/S314E-FVII, F374Y/L305VA/158D/E296V/M298Q/S314E-FVII,F374Y/L305V/E296V/M298QA/158T/S314E-FVII, F374Y/L305V/E296V/M298Q/K337AA/158T-FVII, F374Y/L305V/E296V/K337AA/158T/S314E-FVII, F374Y/L305V/M298Q/K337AA/158T/S314E-FVII, F374Y/L305VA/158D/E296V/M298Q/K337A-FVII, F374Y/L305VA/158D/E296V/K337A/S314E-FVII,F374Y/L305VA/158D/M298Q/K337A/S314E-FVII,F374Y/L305V/E296V/M298Q/K337AA/158T/S314E-FVII, F374Y/L305VA/158D/E296V/M298Q/K337A/S314E-FVII, S52A-Factor VII, S60A-Factor VII; R152E-Factor VII, S344A-Factor VII, Factor Vila lacking the Gla domain; and P11Q/K33E-FVII, T106N-FVII, K143N/N145T-FVII, V253N-FVII, R290N/A292T-FVII, G291N-FVII, R315N/V317T-FVII, K143N/N145T/R315NA/317T-FVII; and FVII having substitutions, addi-tions or deletions in the amino acid sequence from 233Thr to 240Asn, FVII having substitutions, additions or deletions in the amino acid sequence from 304Arg to 329Cys. Growth hormone (GH) applicable in the methods of the present invention includes human growth hormone (hGH), which sequence and characteristics are set froth in, e.g. Hormone Drugs, Gueriguian, U.S.P. Covention, Rockvill, 1982 and growth hormone com-pounds. The term "growth hormone compound" is intended to indicate human growth hormone (hGH) in which one or more amino acid residues have been deleted and/or replaced by other amino acid residues, natural or unnatural, and/or hGH comprising addition amino acid residues, natural or unnatural, and/or hGH in which at least one organic substituent is bound to one or more organic substituent. Particular mentioning is made of the 191 native amino acid sequence (somatropin) and the 192 amino acid N-terminal methionine species (somatrem). Other examples of growth hormone compound applicable in the present invention include wherein amino acid No 172, 174,176 and 178 as a group are replaced by one of the following groups of amino acids (R, S, F, R); (R, A, Y, R), (K, T, Y, K); (R, S, Y, R); (K, A, Y, R); (R, F, F, R); (K, Q, Y, R); (R, T, Y, H); (Q, R, Y, R); (K, K, Y, K); (R, S, F, S) or (K, S, N, R) as disclosed in WO 92/09690 (Genentech), which is incorporated herein by reference. Other examples of growth hormone compound applicable in the present invention include hGH with the following substitutions G120R, G120K, G120Y, G120F and G120E, as disclosed in US 6,004931 (Genentech), which is incorporated herein by reference. Other examples of growth hormone compound applicable in the present invention include hGH with the following set of substitutions R167N, D171S, E174S, F176Y and I179T; R176E, D171S, E174S and F176Y; F10A, M14W, H18D and H21N; F10A, M14W, H18D, H21N, R167N, D171S, E174S, F176Y, I179T; F10A, M14W, H18D, H21N, R167N, D171A, E174S, F176Y, I179T; F10H, M14G, H18N and H21N; F10A, M14W, H18D, H21N, R167N, D171A, T175T and I179T; and F10I, M14Q, H18E, R167N, D171S and I179T, as disclosed in US 6,143,523 (Genentech), which is incorporated herein by reference. Other examples of growth hormone compound applicable in the present invention include hGH with the following set of substitutions H18A, Q22A, F25A, D26A, Q29A, E65A, K168A, E174A and G120K as disclosed in US 6,136,536 (Genentech), which is incorporated herein by reference. Other examples of growth hormone compound applicable in the present invention include hGH with the following set of substitutions H18D, H21N, R167N, K168A, D171S, K172R, E174S, I179T and wherein G120 is further substituted with either R, K, W, Y, F or E, as disclosed in US 6,057,292 (Genentech), which is incorporated herein by reference. Other examples of growth hormone compound applicable in the present invention include hGH with the following set of substitutions H18D, H21N, R167N, K168A, D171S, K172R, E174S and I179T, as disclosed in US 5,849,535 (Genentech), which is incorporated herein by reference. Other examples of growth hormone compound applicable in the present invention include hGH with the following set of substitutions H18D, H21D, R167N, K168A, D171S, K172R, E174S and I179T; and H18A, Q22A, F25A, D26A, Q29A, E65A, K168A and E174A, as disclosed in WO 97/11178 (Genentech), which is incorporated herein by reference. Other examples of growth hormone compound applicable in the present invention include hGH with the following set of substitutions K168A and E174A; R178N and I179M; K172A and F176A; and H54F, S56E, L58I, E62S, D63N and Q66E as disclosed in WO 90/04788 (Genentech), which is incorporated herein by reference. Examples of cytokines which could be modified using the rnethod of the present in-vention include erythropoietin (EPO), thrombopoietin, INF-a, IFN-p, IFN-y, TNF-a, interleukin-1p (IL-1-P), IL-3, IL-4, IL-5, IL-10, IL-12, IL-15, IL-18, IL-19, IL-20, IL-21 IL-24, grannolyte col-ony-stimulating factor (G-CSF), GM-CSF, and chemokines such as machrophage inflamma-tory protein-1 (MIP-1) gamma interferon inducible protein and monokines induced by IFNy (MIG). Particular examples of IL-19 applicable in the methods of the present invention include those disclosed WO 98/08870 (Human Genome Science), which is incorporated herein by reference. Particular mentioning is made of the peptide disclosed as SEQ ID NO:2 in WO 98/08870. Particular examples of applicable IL-20 include those disclosed in WO 99/27103 (Zy-mogenetics), which is incorporated herein by reference. In the present context, IL-20 is in-tended to indicate IL-20 itself and fragments thereof as well as polypeptides being at least 90% identical to IL-20 or fragments thereof. Proteins particular applicable in the methods of the present invention includes those disclosed in WO 99/27103 as SEQ ID NO:1, SEQ ID N0:2, SEQ ID N0:3, SEQ ID N0:4, SEQ ID NO:5, SEQ ID NO:6, SEQ ID NO:7, SEQ ID N0:8, SEQ ID N0:9, SEQ ID N0:10, SEQ ID N0:11, SEQ ID NO:12, SEQ ID N0:13, SEQ ID N0:14, SEQ ID NO:15, SEQ ID NO:16, SEQ ID NO:17, SEQ ID NO:18, SEQ ID NO:19, SEQ ID NO:20, SEQ ID N0:21, SEQ ID NO:22, SEQ ID N0:23, SEQ ID N0:24, SEQ ID N0:25, SEQ ID NO:26, SEQ ID N0:27, SEQ ID N0:28, SEQ ID NO:29, SEQ ID NO:30, SEQ ID NO:31, SEQ ID NO:32, SEQ ID NO:33, SEQ ID NO:34 and SEQ ID NO:35. Examples of IL-21 applicable in the methods of the present invention include those disclosed in WO 00/53761 (Zymogenetics), which is incorporated herein by reference. particular mentioning is made of the peptide disclosed as SEQ ID NO:2 in WO 00/53761. TTF are applicable in the methods of the present invention. TTF peptides are a family of peptides found mainly in association with the gastrointestinal tract. Particular mentioning is made of breast cancer associated pS2 peptide (TFF-1), which is known from human, mouse, and rât, spasmolytical polypeptide (TFF-2), which is known from human, pig, rât, and mouse and intestinal trefoil factor (TFF-3), known from human, rât and mouse. Other peptides from the TFF family applicable in the methods of the present invention include those disclosed in WO 02/46226 (Novo Nordisk), which is included herein by reference. Particular mentioning is made of a TFF-2 peptide wherein a TFF2 peptide with an amino acid as disclosed in SEQ ID NO:1 of WO 02/46226 comprising disulphide bonds be- tween Cys6-Cys104, Cys8-Cys35, Cys19-Cys34, Cys29-Cys46, Cys58-Cys84, Cys68-Cys83, and Cys78-Cys95 and wherein a moiety X independently selected from sugar resi-dues and oligosaccharides is covalently attached to Asn15. Other peptides of the TFF family include TFF-1 and TFF-3 dimers as those disclosed in WO 96/06861 (Novo Nordisk), which is incorporated herein by reference. Several melanorcortin receptors are known, and particular mentioning of peptides applicable for the methods of the present invention is made of peptidic melanocortin-4 receptor agonists, which are known to have an appetite suppressive effect. Particular mentioning is made of peptides or proteins disclosed in the following patent documents, which are all incorporated herein by reference: US 6,054,556 (Hruby), WO 00/05263 (William Harvey Research), WO 00/35952 (Melacure), WO 00/35952 (Melacure), WO 00/58361 (Procter & Gamble), WO 01/52880 (Merck), WO 02/26774 (Procter & Gamble), WO 03/06620 (Palatin), WO 98/27113 (Rudolf Magnus Institute) and WO 99/21571 (Trega). Other classes of peptides or proteins which are applicable in the methods of the present invention include enzymes. Many enzymes are used for various industrial purposes, and particular mentioning is made of hydrolases (proteases, lipases, cellulases, esterases), oxi-doreductases (laccases, peroxidaxes, catalases, superoxide dismutases, lipoxygenases), transferases and isomerases. Other peptides or proteins applicable in the methods of the present invention include ACTH, corticotropin-releasing factor, angiotensin, calcitonin, insulin and fragments and ana-logues thereof, glucagon, IGF-1, IGF-2, enterogastrin, gastrin, tetragastrin, pentagastrin, urogastrin, epidermal growth factor,, secretin, nerve growth factor, thyrotropin releasing hormone, somatostatin, growth hormone releasing hormone, somatomedin, parathyroid hor-mone, thrombopoietin, erythropoietin, hypothalamic releasing factors, prolactin, thyroid stimulating hormones, endorphins, enkephalins, vasopressin, oxytocin, opiods and ana-logues thereof, asparaginase, arginase, arginine deaminase, adenosine deaminase and ri-bonuclease. Peptides to be modified according to the methods of the present invention may either be isolated from natural sources (e.g. plants, animals or micro-organisms, such as yeast, bacteria, fungi or vira) or they may be synthesised. Peptides form natural sources also include peptides form transgenic sources, e.g. sources which have been genetically modified to express or to increase the expression of a peptide, wherein said peptide may be "natural" in the sense that it exists in nature or "unnatural" in the sense that it only exists due to human intervention. Peptides isolated form natural sources may also be subjected to synthetic modi-fication prior to the conjugation of the present invention. In one embodiment, the invention relates to conjugated peptides obtainable, such as obtained according to the methods of the present invention. If the conjugated peptide obtainable, such as e.g. obtained by the methods of the present invention is a therapeutic peptide, the invention also provides the use of such compounds in therapy, and pharmaceutical com-positions comprising such compounds. In one embodiment, the invention provides conjugated peptides of the formula wherein P, R, A, D, E and Z are as defined above, and wherein the group (Formula Removed) represents a peptide radical obtained by removing a hydrogen from -NH2 in the side chain of a Gin residue, and pharmaceutically acceptable salts, solvates and prodrugs thereof. In particular, the compound according to the formula represents human growth hormone which has been conjugated at position 141, and in particular exclusively ar this site. Particular examples of such compounds include NEl41-[2-(4-(4-(mPEG(20k)ylbutanoyl)-amino-butyloxyimino)-ethyl]hGH, Ne141-[2-(1-(hexadecanoyl)piperidin-4-yl)ethyloxyimino)-ethyl]hGH, N£l41(2-(4-(4-(1,3-bis(mPEG(20k)ylaminocarbonyloxy)prop-2-yloxy)butyrylamino)butyloxyimino)ethyl)hGH, NEl41(2-(4-(2,6-bis(mPEG(20k)yloxycarbonylamino)hexanoylamino)butyloxyimino)ethyl)hGH, NEl41(2-(4-(4-(mPEG(30k)yloxy)butyrylamino)butyloxyimino)ethyl)hGH, N£l41(2-(4-(4-(mPEG(20k)yloxy)butyrylamino)butyloxyimino)ethyl)hGH, and N£l41(2-(4-(3-(mPEG(30k)yloxy)propanoylamino)butyloxyimino)ethyl)hGH; and pharmaceutically acceptable salts, solvates and prodrugs thereof. As discussed above, mPEG(20k)yl mentioned in the above list is intended to indicate mPEG(20k)yl with a polydispersity index below 1.06, such as below 1.05, such as below 1.04, such as below 1.03, such as between 1.02 and 1.03. Simialrly, mPEG(30k)yl mentioned in the above list is intended to indicate mPEG(30k)yl with a polydispersity index below 1.06, such as below 1.05, such as below 1.04, such as below 1.03, such as between 1.02 and 1.03. As discussed above, a peptide may contain more than one Gln-residue where the peptide can be conjugated. In that case, the above formula is intended also to indicate a peptide which has been conjugated at more than one site. To the extend that the unconjugated peptide (P-C(O)-NH2) is a therapeutic peptide, the invention also relates to the use of the the conjugated peptides l therapy, and in particular to pharmaceutical compositions comprising said conjugated peptides. Insulin is used to treat or prevent diabetes, and in one embodiment, the present invention thus provides a method of treating type 1 ortype 2 diabetes, the method comprising administering to a subject in need thereof a therapeutically effective amount of an insulin or insulin compound conjugate according to the present invention. In another embodiment, the invention provides the use of an insulin or insulin compound conjugate according to the present invention in the manufacture of a medicament used in the treatment of type 1 or type 2 diabetes. GLP-1 may be used in the treatment of hyperglycemia, type 2 diabetes, impaired glucose tolerance, type 1 diabetes, obesity, hypertension, syndrome X, dyslipidemia, (3-cell apoptosis, (3-cell deficiency, inflammatory bowel syndrome, dyspepsia, cognitive disorders, e.g. cognitive enhancing, neuroprotection, atheroschlerosis, coronary heart disease and other cardiovascular disorders. In one embodiment, the present invention thus provides a method of treating said diseases, the method comprising administering to a subject in need thereof a therapeutically effective amount of a GLP-1 or GLP-1 compound conjugate according to the present invention. In another embodiment, the invention provides the use of a GLP-1 or GLP-1 compound conjugate according to the present invention in the manufacture of a medicament used in the treatment of the above mentioned diseases. GLP-2 may be used in the treatment of intestinal failure leading to malabsorption of nutrients in the intestines, and in particular GLP-2 may be used in the treatment of small bowel syndrome, Inflammatory bowel syndrome, Crohns disease, colitis including collagen colitis, radiation colitis, post radiation atrophy, non-tropical (gluten intolerance) and tropical sprue, damaged tissue after vascular obstruction or trauma, tourist diarrhea, dehydration, bacteremia, sepsis, anorexia nervosa, damaged tissue after chemotherapy, premature in-fants, schleroderma, gastritis including atrophic gastritis, postantrectomy atrophic gastritis and helicobacter pylori gastritis, ulcers, enteritis, cul-de-sac, lymphatic obstruction, vascular disease and graft-versus-host, healing after surgical procedures, post radiation atrophy and chemotherapy, and osteoporosis. It is therefore an intension of the present invention to pro-vide methods of treating the above diseases, the method comprising administering to a sub-ject in need thereof a therapeutically effective amount of a GLP-2 or GLP-2 compound conjugate according to this invention. In another embodiment, the present invention provides the use of a GLP-2 or GLP-2 compound conjugate according to this invention in the manufacture of a medicament used in the treatment of the above mentioned diseases. Growth hormone may be used in the treatment of growth hormone deficiency (GHD); Turner Syndrome; Prader-Willi syndrome (PWS); Noonan syndrome; Down syn-drome; chronic renal disease, juvenile rheumatoid arthritis; cystic fibrosis, HlV-infection in children receiving HAART treatment (HIV/HALS children); short children born short for gesta-tional age (SGA); short stature in children born with very low birth weight (VLBW) but SGA; skeletal dysplasia; hypochondroplasia; achondroplasia; idiopathic short stature (ISS); GHD in adults; fractures in or of long bones, such as tibia, fibula, femur, humerus, radius, ulna, clavicula, matacarpea, matatarsea, and digit; fractures in or of spongious bones, such as the scull, base of hand, and base of food; patients after tendon or ligament surgery in e.g. hand, knee, or shoulder; patients having or going through distraction oteogenesis; patients after hip or discus replacement, meniscus repair, spinal fusions or prosthesis fixation, such as in the knee, hip, shoulder, elbow, wrist or jaw; patients into which osteosynthesis material, such as nails, screws and plates, nave been fixed; patients with non-union or mal-union of fractures; patients after osteatomia, e.g. from tibia or 1st toe; patients after graft implantation; articular cartilage degeneration in knee caused by trauma or arthritis; osteoporosis in patients with Turner syndrome; osteoporosis in men; adult patients in chronic dialysis (APCD); malnu-tritional associated cardiovascular disease in APCD; reversal of cachexia in APCD; cancer in APCD; chronic abstractive pulmonal disease in APCD; HIV in APCD; elderly with APCD; chronic liver disease in APCD, fatigue syndrome in APCD; Crohn's disease; impaired liver function; males with HIV infections; short bowel syndrome; central obesity; HlV-associated lipodystrophy syndrome (HALS); male infertility; patients after major elective surgery, alco-hol/drug detoxification or neurological trauma; aging; frail elderly; osteo-arthritis; traumatically damaged cartilage; erectile dysfunction; fibromyalgia; memory disorders; depression; traumatic brain injury; subarachnoid haemorrhage; very low birth weight; metabolic syndrome; glucocorticoid myopathy; or short stature due to glucucorticoid treatment inchildren. Growth hormones have also been used for acceleration of the healing of muscle tissue, nervous tis-sue or wounds; the acceleration or improvement of blood flow to damaged tissue; or the de- crease of infection rate in damaged tissue, the method comprising administration to a patient in need thereof an effective amount of a therapeutivcally effective amount of a compound of formula I. The present invention thus provides a method fortreating these diseases or states, the method comprising administering to a patient in need thereof a therapeutically effective amount of a growth hormone or growth hormone compound conjugate according to the present invention. Typically, the amount of conjugated growth hormone administered is in the range from 1