PL157648B1 - The method of peptide derivative manufacture - Google Patents

Abstract

1 . A method for preparing new derivatives of peptides of formula 1, in which P is the residue of a biologically active peptide of formula NH 2-P, having hormonal action, hormonal inhibitory action, enzymatic action, inhibitory enzymatic action or immunomodulatory action, especially somatostatin, calcitonin, oxytocin, vasopressin, LH, LHRH, G RF, gastrin, substance P, cathepsin, encephalin or their derivatives or analogues with a similar or antagonizing effect, the NH group is located at the N-terminus or in the side chain of the peptide; X denotes a sugar residue attached to the amino group by a bond other than a direct N-glycosidic bond of the formula la, which denotes a deoxyketose residue, of formula 2a, which denotes a deoxyaldose residue, of formula 3a, which denotes a uronic acid or polyhydroxymono- or dicarboxylic acid residue , of formulas 4a',4b',4c',4d', 5a' and 5b', in which Q, Q', Q" and Q"' denote groups binding the peptide moiety to the sugar moiety, Y is H 2 or H, OH, c is 2, 3 or 4, and any of the free hydroxyl groups in the polyol groups of residues of formulas 5a' and 5b' are optionally glycosyl-linked to a reducing mono-, di-or oligosaccharide or amino sugar, and addition salts with acid and complexes of these peptide derivatives, provided that a) in compounds of formula 1, in which X is a sugar moiety of formula Ia, . . . (and independent claims 6, 7). PL PL PL

Description

REPUBLIC POLAND © PATENT DESCRIPTION @ PL © 157648 © Bl 0 Application No. ^N: 285052 ( ⁵¹ ) IntCl® ^: C07K 9/00 Patent Office of the Republic of Poland Date of notification: October 12, 19 ⁸⁷ READING 9 FIELO A

Method for the production of new peptide derivatives

Number of the application from which the separation took place:

268173

The holder of the patent:

Sandoz A.G., Basel, CH

Priority:

1986-10-13, DE, P.3634797.3

October 13, 1986, D E, P.3634825.2

October 13, 1986, DE, P.3634826.0 04/14/1987, DE, P.3712626.1

Proxy:

PATPOL Spółka z 0.0., Warsaw, PL

Application announced:

September 1, 1988 BUP 18/88

The grant of the patent was announced on: June 30, 1992 WUP 06/92

PL 157648 Bl

1, A method for the preparation of new peptide derivatives57) of the formula I, in which P is the residue of a biologically active peptide of formula NH2-P, showing a hormonal, hormonal, enzymatic, inhibitory or immunomodulatory effect, especially somatostatin, calcitonin, oxytocin, vasopressin, LH, LHRH, GRF, gastrin, substance P, cathepsin, encephalin or derivatives or analogues thereof having a similar or antagonizing effect, the NH group is at the N-terminus or in the side chain of the peptide; X is a sugar residue attached to the amino group other than a direct N-glycosidic bond of formula Ia which is a deoxyketose residue of formula 2a which is a deoxyaldose residue of formula 3a which is a uronic acid or polyhydroximono- or dicarboxylic acid residue, with the formulas 4a ', 4b', 4c ', 4d', 5a 'and 5b', where Q, Q ', Q and Q' are groups linking the peptide residue to the sugar residue, Y is H2 or H, OH, c is number 2, 3 or 4, and any of the free hydroxyl groups in the polyol groups of residues of formulas 5a 'and 5b' is optionally glycosylated to a reducing mono-, di-, or oligosaccharide or amino sugar, and acid addition salts and complexes of these peptide derivatives with the proviso that a) in compounds of formula 1 in which X is a sugar moiety of formula Ia, ... (and independent claims 6, 7).

X-NH - P

MODEL 1

Method for the production of new peptide derivatives

Claims (3)

Patent claims 1. Method for the preparation of new peptide derivatives of formula 1, in which P is the residue of a biologically active peptide of formula NH2-P, showing hormonal, hormonal, enzymatic, enzymatic inhibitory or immunomodulating effects, especially somatostatin, calcitonin, oxytocin, vasopressin, LH, LHRH, GRF, gastrin, substance P, cathepsin, encephalin or derivatives or analogues thereof having a similar or antagonizing effect, the NH group is at the N-terminus or in the side chain of the peptide; X is a sugar residue attached to the amino group other than a direct N-glycosidic bond of formula Ia which is a deoxyketose residue of formula 2a which is a deoxyaldose residue of formula 3a which is a uronic acid or polyhydroximono- or dicarboxylic acid residue, with the formulas 4a ', 4b', 4c ', 4d', 5a 'and 5b', where Q, Q ', Q and Q' are groups linking the peptide residue to the sugar residue, Y is H2 or H, OH, c is the number 2, 3 or 4, and any of the free hydroxyl groups in the polyol groups of residues of formulas 5a 'and 5b' is optionally glycosylated to a reducing mono-, di-, or oligosaccharide or amino sugar, and acid addition salts and complexes of these peptide derivatives provided that a) in compounds of formula I, in which X is a sugar residue of formula Ia, P is a radical other than the gastrin radical with a C-terminal group terminating in -Asp-Phe-NFb, b) when the residue of formula 3a represents the residue of an optionally N-acylated muramino acid the second amino acid residue from the N-terminus of the P-NH2 peptide should be a residue other than an aminodicarboxylic acid residue, characterized in that the peptide of formula P-NH2, as defined above, in protected or unprotected form, is reacted with a sugar containing at least one sugar residue of the formula Ia, 2a, 3a, 4a ', 4b', 4d ', 5a' or 5b 'as defined above, optionally in protected form, and if the resulting compound contains at least one protecting group, this group is removed and the resulting compound is isolated in free form, as acid addition salt or as a complex. 2. The method according to p. A method according to claim 1, characterized in that the biologically active peptide is a peptide of formula 8 in which A is hydrogen, an alkyl of 1 to 3 carbon atoms or an alkanoyl of 1 to 4 atoms, the group N-CH (Zi) -Co is 1) an (L) - or (D) -phenylalanine residue, optionally substituted with halogen, NO2, NH2, OH, alkyl containing 1 to 3 carbon atoms and / or alkoxy containing 1 to 3 carbon atoms, or 2) a natural lipophilic σ-amino acid residue or of a suitable (D) -amino acid other than specified in item 1), and Z1 in the group> N-CH (Zi) -CO- means the amino acid residue specified in items 1) and 2), A 'is hydrogen or an alkyl containing 1 up to 3 carbon atoms, Y1 and Y2 are each independently 1) hydrogen, 2) a group of formula 24 in which m is an integer from 1 to 4, Ra is CH3 or C2H5 and Rb is H, CH3 or C2H5 or 3) a group of formula 25 in which n is an integer from 1 to 5 or 4) a group -CO-NHRc in which Rc is a straight or branched alkyl radical, includes containing 1 to 6 carbon atoms or 5) a group of formula 26, in which Rd is a natural σ-amino acid residue with hydrogen, which is placed on the carbon atom a, Ra is an alkyl radical containing 1 to 3 carbon atoms or 6) a group of the formula 27, wherein Ra 'and Rb' are independently hydrogen, CH3 or C2H5, Re and R9 are independently hydrogen, F, Cl, Br, alkyl of 1 to 3 carbon atoms or alkoxy of 1 to 3 carbon atoms, p is 0 or 1, q is 0 or 1, and r is 0, 1 or 2 or Y1 and Y2 together represent a bond, B is Phe, optionally substituted in the phenyl radical with F, Cl, Br, NO2, NH2, OH, alkyl containing 1 to 3 carbon atoms or alkoxy containing 1 to 3 carbon atoms, C is L- or D-Trp, optionally substituted in the benzene ring with F, Cl, Br, NO2, NH2, OH, alkyl containing 1 to 3 carbon atoms or alkoxy containing 1 to 3 carbon atoms, D is Lys, in which the σ-amino group may be substituted with methyl, F is Thr, Ser, Val, F oz is COOR1, CH2OR.2, CO-NR3R4 or a group of formula 28, R1 is hydrogen or alkyl containing 1 to 3 carbon atoms, R2 is hydrogen or the remainder of a physiologically acceptable and physiologically hydrolysable ester, R3 is hydrogen, alkyl containing 1 to 3 carbon atoms, phenyl 157 648 or phenylalkyl having 7 to 10 carbon atoms with the proviso that when R4 is -CH (R.3) -Xi then R3 is only hydrogen or methyl, R4 is hydrogen, alkyl of 1 to 3 carbon atoms or of formula 9, R5 represents a natural amino acid residue with hydrogen which is placed on carbon a or a radical HO-CH2-CH2- or HO (-CH2) 3, wherein the group of formula 9 may have the L- or D- configuration , Χ1 is COOR1, CH2OR2 or CONR6R7, Re is hydrogen or alkyl containing 1 to 3 carbon atoms, R7 is hydrogen, alkyl containing 1-3 carbon atoms, phenyl or phenylalkyl containing 7 to 10 carbon atoms, with residues B, D and F are in L-form and the residues at positions 2 and 7 as well as the residues Yi4 / and Y24 / independently exist in D- or L-form. 3. The method according to p. A process as claimed in claim 1, characterized in that in the preparation of N ^g - (q-glucosyl / 13) -deoxyfructosyl) - (D) -Phe-Chys-Phe- (D) -Trp-Lys-Thr-Cys-Thr-ol H- DPhe-Chys-Phe-DTrpLys (Boc} -Thr-C ^ s-Thr-ol is reacted D (+ imaltose and then the protecting group is removed. 4. The method according to p. A method according to claim 1, characterized in that the biologically active peptide is calcitonin of formula 10, in which R is R'CO or H, RCO is an acyl radical of a carboxylic acid, Y / is a radical at the σ-Ca-amino acid atom, Y2 'is a radical placed at the σ-Ca-amino acid atom, a group of the formula -CH2-SS-CH2-OH (NH2) -COOH, -CH2S-S-CH2-CH2-COOH, - (CH2) s-COOH or -CH2-S- Y3, Y3 is an alkyl of 1 to 4 carbon atoms, benzyl optionally substituted with methyl or methoxy or a group of formula CH3CONH-CH2-, o is an integer from 1 to 4, Ae is Thr or D-Thr, s is an integer from 3 to 5, Ae is the aminoacyl radical of a neutral, lipophilic L-α amino acid, A9 is the aminoacyl radical of a neutral, lipophilic L- or Β-σ-amino acid, and Zi is a polypeptide radical located in positions 10 to 31 of a natural calcitonin or a derivative or analog thereof showing activity hypocalcemic, wherein the radicals Y1 'in formula 10, independently of each other, may be the same l or the different and all amino acid radicals in formula 10, except the aminoacyl radical Ae, may have the L or D configuration. 5. The method according to p. The process of claim 1, wherein the Amadori or Heyns rearrangement is performed when X is a residue of the formula Ia, 2a, 4c 'or 4d' for the preparation of compounds of formula I. 6. A method for the preparation of new derivatives of peptides of formula 1, in which P is a group of formula 30, the N-CH (Z) -CO group is 1) optionally via halogen, NO2, NH2, OH, alkyl with 1-3 carbon atoms and / or alkoxy with 1-3 carbon atoms, substituted (L) - or (D) -phenylalanine radical, or 2) a radical other than 1) given, of a natural lipophilic amino acid, where Z in the> N-CH (Z) - moiety CO- is a radical of the amino acid radicals defined under 1) and 2), A is hydrogen or alkyl of 1-3 carbon atoms, Y1 and Y2 independently represent 1) hydrogen, 2) a group of formula 24, in which m is the number an integer 1-4, Ra is CH3 or C2H5 and Rb is hydrogen, CH3 or C2H5, or 3) a group of formula 25 where n is an integer 1-5, or 4) a -CO-NHRc group in which Rc is a straight-chain or branched alkyl radical with 1-6 carbon atoms, or 5) a group of formula 26, wherein Rd is a radical of a natural σ-amino acid (including hydrogen) located on the σ-atom and Re is an alkyl radical of 1-5 carbon atoms, 6) a group of formula 27 in which Ra and Rb are independently of each other hydrogen, CH3 or C2H5, Re and R9 are independently of each other hydrogen, F, Cl, Br, alkyl of 1-3 carbon atoms or alkoxy of 1-3 carbon atoms, p is 0 or 1, q is 0 or 1, r is 0, 1 or 2, or Y1 and Y2 together form a bond, B is a group Phe or the Phe group substituted in the phenyl radical by F, Cl, Br, NO2, NH2, OH, alkyl of 1-3 carbon atoms or alkoxy of 1-3 carbon atoms, C is optionally in the benzene ring by F, Cl, Br, NO2, NH2, alkyl with 1-3 carbon atoms or alkoxy with 1-3 carbon atoms substituted with L- or D-Trp group, D is Lys group, the aamino group may be substituted by methyl, E is Thr group, Ser, Val, F is COOR1, CH2OR2, CO-NH3R4 or a group of formula 28 in which Xi is X, Ri is hydrogen or alkyl with 1-3 carbon atoms, R2 is hydrogen or a physiologically acceptable radical other physiologically hydrolysable ester, R3 is hydrogen, alkyl of 1-3 carbon atoms, phenyl or phenylalkyl of 7-10 carbon atoms, however in the case of R4 being -CH (Rs) -X, R3 is only hydrogen or methyl , R4 is hydrogen, alkyl with 1-3 carbon atoms or a group of formula -CH (Rs) -X, R5 is CH2OH, - (CH2) zOH, - (CH2) 3OH or a substituent attached to a4 157,648 natural carbon atom of a σ-amino acid (including hydrogen), wherein the group -CH (Rs) -X may be in the -L or -D configuration. X is COORi, CH2OR2 or CON (ReR7), R7 is hydrogen or alkyl of 1-3 carbon atoms, R7 is hydrogen, alkyl of 1-3 carbon atoms, phenyl or phenylalkyl of 7-10 carbon atoms, the radicals B , D and E may be in the -L form, and the radicals in the -2 and -7 position and the radicals Yi4 / and Y24 / may be in the -D or -L form, X in formula 1 is a deoxidative of ketose or corresponding uronic acid, attached to the -NH- group via the -CH2- group, obtained as a result of the Amadori rearrangement of the aldose or the corresponding uronic acid with a free amino group of the polypeptide radical of the compound of formula 1 or X is the acyl radical of uronic acid, polyhydroxycyclohexanecarboxylic acid, N-acetyluraminic or N-acetylneuraminic or X is the residue Qi-CC _n iH2 (nii, where Qi is hydrogen or a glycosyl residue of a mono-, di- or oligosaccharide and ni is an integer of 1-6 and acid addition salts and complexes of these derivatives, characterized in that the protected peptide is in a slightly acidic medium is reacted (Amadori reaction) with a reducing mono-, di- or oligosaccharide, and then at least one protecting group which is present in the protected polypeptide is removed and the compounds thus obtained are optionally converted into their addition salts with acids or their complexes. 7. A method for the preparation of new peptide derivatives of formula 1, in which P represents the residue of a biologically active peptide of formula NH2-P, where the NH group occupies a position at the N-terminus or side chain of the P polypeptide, X represents a group of formula 31, which is a reducing mono-, di- or oligosaccharide residue or the corresponding glucuronic acid or aminosugar, or X is a group of formula 32 which is linked via a -CH2 group to the group -NH- of a biologically active peptide ketose deoxy radical or the corresponding uronic acid formed in as a result of an Amadori rearrangement of an aldose or the corresponding uronic acid with a free amino group of the polypeptide, or X is a group of formula 33, which is a -CH2- linked to the group -NH- of a biologically active peptide of an aldose resulting from a Heyns rearrangement with a free amino group of the polypeptide, or X is a group of formula C4-CO-, where G4 is a uronic acid residue, polyhydroxymono- or dicarboxylic acid, or X represents groups of formula 34, 35 or 36, in which G6, G'6, G6 are sugar radicals and Q ', Q and Q' are peptide linking groups with sugar radical and acid addition salts and complexes of these derivatives, provided that 1) if in the above-mentioned compounds of formula I, X represents a group of formula 31 or G4-CO-, then P cannot be a radical of formula X'-Pre-Phe-Phe-Y'- Z ', where X' and Z 'are D-isomers of natural σ-amino acids, and Y' is a natural α-amino acid, 2) if X in the above-mentioned compounds of formula 1 X represents a group of formula 32, P cannot be a peptide radical gastric, 3) if in the compounds of formula 1 X represents a group of formula 34, in which Q 'is a group of formula -CH (CH3) -CO-L-Ala-D-iso-Gln, then P cannot represent a natural radical somatostatin, characterized in that the protected peptide is reacted with a reducing mono-, di- or polysaccharide or with the appropriate uronic acid to produce compounds of formula I, in which X represents groups of formulas 34, 35 and 36, or the polypeptide is first reacted with the bridge member and then the reaction product is reacted with sugar, or the sugar is first reacted with the bridge member and then the glycosylated bridge member is then reacted with the polypeptide, followed by removal of the protecting groups. The subject of the invention is a process for the preparation of new peptide derivatives suitable for the production of pharmaceuticals. The method of the invention produces derivatives of sugars and biologically active peptides with a prolonged duration of action compared to unmodified sugar peptides, containing at least one sugar residue that is linked to the amino group of at least one amino acid by a linkage other than a direct N-glycosidic bond, and furthermore, if these derivatives are the condensation product of a sugar component containing a carboxyl group and a peptide containing less than 8 amino acid residues, by a linkage other than direct amine linkage. Peptides not modified with sugar are understood to mean peptides which contain no sugar or sugar residues in their structure. They are hereinafter referred to as unmodified peptides. The compounds according to the invention have been found to exhibit particularly interesting and unexpected pharmacological properties, a longer duration of action, as described below. It has been found that these properties are brought about by the inclusion of sugar residues, even linked in a manner other than conventional glycosylation with e.g. Asp or Ser. Preferably, these sugar residues are introduced into the amino groups of the amino acids remote from the peptide's center of activity. The term "peptides" as used herein includes peptides (e.g., di-, tripeptides), oligopeptides, polypeptides, and proteins. Preferably the peptides contain more than 7 amino acid units. The term Amino acid unit also includes amino alcohol units, e.g., reduced amino acids. The term "biologically active peptides" as used herein refers to particular compounds that exhibit pharmacological or therapeutic activity, e.g., compounds that exhibit hormonal, enzymatic or immunomodulatory activity, or that stimulate or inhibit such activity. These biologically active peptides include natural peptides isolated from natural cells or from fermented cells, e.g. genetically engineered or synthesized peptides, as well as derivatives or analogs thereof. Derivatives and analogs are understood to mean especially natural peptides in which one or more amino acid residues have been omitted and / or replaced by one or more other amino acid radicals and / or in which one or more functional groups have been replaced by one or more other functional groups and / or in which one or more groups have been replaced by one or more isosteric groups. Typically, the term includes all modified derivatives of biologically active peptides which exhibit a qualitatively similar effect to that of the unmodified peptides. The sugars used can be, for example, any known mono- or oligosaccharides, especially mono-, di- or trioses or their derivatives, e.g. amino- and / or carboxylic acids and / or reduced and / or resterified derivatives. The sugar may be conjugated, for example, to an N-terminal amino group and / or to at least one amino group present on the side chain of the peptide. The sugar may be linked to the peptide by one of its functional groups directly or indirectly via a bridging member, e.g., an alkylene carbonyl group. Such coupling may be performed by a conventional method, especially as described below. In a preferred group of compounds according to the invention, the sugar residue is linked to the amino group of the peptide via a linkage other than a direct N-glycosidic bond or a direct amide bond. The compounds according to the invention, especially those having at least 8 amino acid units, are suitable for the preparation of oral pharmaceuticals. The method according to the invention produces sugar derivatives of biologically active peptides of formula I, in which P is the residue of a biologically active peptide having a hormonal, hormonal, enzymatic, enzymatic, or immunomodulatory effect, e.g. somatostatin, calcitonin, oxytocin, vasopressin, LH, LHRN, GRF, gastrin, substance P, cathepsin, encephalin or derivatives or analogues similar or antagonizing of the formula NH2-P wherein the NH group is at the N-terminus or side chain of the peptide; X represents a non-direct N-glycosidic bond attached to the amino group, a sugar residue of formula Ia which is a deoxyketose residue of formula 2a which is a deoxyaldose residue of formula 3a which is a uronic acid or polyhydroximono- or dicarboxylic acid residue, with the formulas 4a ', 4b', 4c ', 4d', 5a 'and 5b', where Q, Q ', Q and Q' are groups linking the peptide residue to the sugar residue, Y is H2 or H, OH, c is a number of 2,3 or 4, with any of the free hydroxyl groups in the polyol groups in compounds of formula 5a 'and 5b' being optionally linked glycosylated to a reducing mono-, di- or oligosaccharide or amino sugar, and the salt Acid addition and complexes of these peptide derivatives, provided that a) in compounds of formula 1 in which X is a sugar residue of formula Ia, P is a radical other than the C-terminal terminated gastrin radical. -Asp-Phe-NH2, b) when the residue of formula 3a (GeCO) is an optionally N-acyl muramic acid residue, then the second amino acid residue from the N-terminus of the P-NH2 peptide should be a residue other than the amino dicarboxylic acid residue. As defined above for compounds of formula I, the scope of this formula includes sugar derivatives of biologically active peptides: a) of general formula Γ, in which X is a group of formula Ia, which is a deoxyketose residue linked by a CH2 group to the NH group of a biologically active peptide, and P is a residue of a biologically active peptide of formula NH2-P, in which the NH group is located at the N-terminus or in the side chain of the P-peptide, b) of formula 2, in which the group of general formula 2a is a deoxyaldose residue bound by a slow bond to the NH group of a biologically active peptide, and P is a residue of a biologically active peptide of formula NH2-P, in which the NH group is at the N-terminus or in the side chain of the P peptide, c) of general formula III, in which G3CO- is a residue of uronic acid or a polyhydroxymono- or dicarboxylic acid, Ry is hydrogen or an alkyl containing 1 to 3 carbon atoms or an alkanoyl containing 1 to 4 carbon atoms, and P is the residue of a biologically active peptide of formula NH2-P containing at least 8 amino acid residues, wherein NRy is at the N-terminus or side chain of the P peptide, d) of general formula 4a, 4b, 4c or 4d, in which P is the residue of a biologically active peptide of formula H2N-P, groups of formulas 4a ', 4b', 4c ', 4d' are sugar residues, Ry is hydrogen, alkyl containing 1 to 3 carbon atoms or an alkanoyl containing 1 to 4 carbon atoms, and Q, Q ', Q and Q' are groups coupling the residue of the peptide to a sugar residue, the NH group being located at the N-terminus or side chain of the peptide, or e) of formula 5a or 5b, in which Y is H2 or H or OH, c is the number 2 or 4, P is the residue of a biologically active peptide of formula H2N-P, wherein the NH group linked to P is at the N-terminus or in the side chain of the P peptide, and any of the free hydroxyl groups in the polyol substituent of the compounds of formula 5 is optionally linked in a glycosylated manner to a reducing mono-, di- or oligosaccharide or amino sugar, and addition salts and complexes of these peptide derivatives are prepared, with the above-mentioned reservation. Gastrin is a peptide that increases gastric acid secretion. All the sugar residues listed above may be mono-, di- or oligosaccharide residues. These sugars can be heptoses, hexoses and / or pentoses, which can be pyranoses or furanoses. The above-defined formulas show compounds in which only one sugar residue is allocated to the remainder of the peptide. However, it is also within the scope of the invention to produce sugar derivatives of peptides containing more than one free amino group per peptide residue, e.g., containing 2 or 3 sugar residues per peptide residue. Sugar polypeptides preferably contain 1 to 3 monosaccharide residues which may be linked together as disaccharides or trisaccharides. In all of the above-mentioned compounds, the ~ line indicates that the bond may be in the α- or β- position. In general formula 1, the group of formula Ia may preferably be a) a residue of formula 60, in which one of the radicals G _a and Gb is hydrogen and the other is the OH group, one of the radicals Gc and Gd is hydrogen, and the other is the OH group, one of the radicals Gc and Gd is hydrogen, and the other the group OH or O-glycosyl, which is a derivative of a reducing mono-, di-oligosaccharide, one of the Ge and Gf radicals is hydrogen and the other the OH group, one of the Gg and Gh radicals is hydrogen and the other is hydrogen or CH2OH, e.g. the residue in which the radicals Ga to Gh are selected such that the residue of formula 6a corresponds to a radical obtainable by Amadori rearrangement from a natural or synthetic mono-, di- or oligosaccharide. As examples of sugar residues of formula 6a, the following residues may be mentioned: deoxyfructose, deoxytagatosyl, deoxyribosyl, α-glucosyl- (1-4) -deoxyfructosol, α-glucosyl- (1-4) -crglucosyl (1-4) -deoxyfructosyl. 157 648 b) the residue of formula 6b, where one of G _a and Gb is hydrogen and the other is OH group, one of Gc and Ga is hydrogen and the other is OH or O-glycosyl, which is a derivative of reducing mono-, di- or oligosaccharide, one of the Ga and Gf radicals is hydrogen and the other is hydrogen, COOH, CH2OH, CH2-OP (O) - (OH) 2 or CH2O-glycosyl in which the glycosyl radical is a derivative of reducing mono-, di - or an oligosaccharide, e.g. a residue in which the radicals Gc to Gf are selected such that the residue of formula 6b corresponds to a radical obtainable by Amadori rearrangement from a natural or synthetic mono-, di- or oligosaccharide. Residues of formula -6b can be obtained, for example, by rearrangement of Amadori from saccharides such as gentobiose, melibiosis, ribose, xylose, or from uronic acids such as glucuronic or galacturic acid. In formula 2, the group of formula 2a is preferably a a) a residue of formula 7a, where one of the Ga or Gb radicals is hydrogen and the other a free bond, one of the Gc or Ga radicals is hydrogen and the other is the OH group, one of the Ge or Gf radicals is hydrogen, and the other is the OH group or O-glycosyl, derived from a reducing mono-, di- or oligosaccharide, one of the radicals Gg and Gh is hydrogen and the other a group CH2OH or CH2-O-glycosyl in which the glycosyl radical is derived from a reducing mono-, di- or oligosaccharide, e.g. a residue in which the radicals Ga to Gh are selected such that the radical of formula 7a corresponds to a radical obtainable by Heyns rearrangement from natural or synthetic mono-, di- or oligoketoses, b) a residue of formula 7b, in which one of the Ga and Gb radicals is hydrogen and the other is a free bond, one of the Gc and Gd radicals is hydrogen, and the other is the OH group, one of the Ge and Gf radicals is hydrogen, and the other is a group CH2OH or a CH2-O-glycosyl group in which the glycosyl radical is a derivative of a reducing mono-, di- or oligosaccharide, e.g. a residue in which the radicals Ga to Gf are selected such that the residue of formula 7b corresponds to the radical obtainable on by Heyns rearrangement from natural or synthetic mono-, di- or oligoketoses. The residues of formula 7a or 7b can be obtained, for example, by Heyns rearrangement from sugars such as D-fructose, lactzole, L-sorbose, D-tagatose or D-ribulose. A. In formula 3, the polyhydroxymono- or dicarboxylic acid, for example, has at least 3 hydroxyl groups, and may also contain other substituents, for example, amino or acetylamino groups. Examples of such polyhydroxycarboxylic acids are: "- onic" acids derived from sugars, such as gluconic acid, or "-aric acids" such as glucaric acid, furthermore quinic acid, acetylmuranoic acid, acetylneuraminic acid or D-glucosamic acid. Examples of uronic acids are glucuronic and galacturonic. In compounds of formulas 4a-4d, G4, G4, G'4 and G'4 are as defined above for G1 or G2. The radical Q or Q 'links the NH2 group of the peptide to the NH2 or OH group of a sugar residue and is e.g. a dicarboxylic acid radical or preferably a radical -CbH2b-CO-, wherein b is the number 0 to 6. The radical may be branched. Q 'is, for example, a radical of the formula 22 or, especially, the radical -CbH2b-CO- b) e.g. is 1 to 6). Q is e.g. the group -CH2-CO-. Q is especially CO- or -CS-. The groups -NH-Q- and -NH-Q 'are radicals which link the NH2 group of a peptide to a sugar residue, especially ω-aminocarboxylic acid radicals. They can be, for example, the radical -NH-C2H2b-CO-. For compounds of formulas 5a and 5b, preferred are compounds of formula 5a, especially in which c is the number 3. All the above-mentioned P residues are biologically active peptide residues. Such peptides include all natural and synthetic peptides (such as derivatives and analogs thereof; see the beginning of the description) having hormonal, enzymatic or immunomodulatory activity. This activity can be both stimulated and inhibited. Examples of such peptides include: somatostatic, calcitonin, oxytocin, vasopressin, insulin, LH, LHRN, GRF, gastrin, substance P, cathepsin, enkephalins, as well as all derivatives and analogues of these peptides which show an activity or effect similar to them. antagonistic. The compounds according to the invention preferably contain at least 8 amino acid residues, e.g. 8 to 32, especially 8 to 20, especially 8 to 10 amino acids. 157 648 Preferred peptides are peptides of general formula Γ and 2. In the formulas shown in the figures, for the sake of simplicity, the sugar radical is usually represented by the pyranose structure. Of course, furanose and open chain structures are also within the scope of the invention, provided they are present in the respective sugars. The process according to the invention for the preparation of compounds of formula I consists in reacting a peptide of formula NH2-O as defined above in protected or unprotected form with a sugar containing at least one sugar moiety of formula Ia, 2a, 3a, 4a. ', 4b', 4d ', 5a' or 5b ', optionally in protected form, and if the obtained compound contains at least one protecting group, this group is removed, and the resulting compound is isolated in free form, in addition salt form with acid or in the form of a complex. According to the invention, a group of compounds of formula I wherein X is a residue of formula Ia, 2a, 4c 'or 4d' can be advantageously prepared by an Amadori or Heyns rearrangement. As mentioned at the beginning of the description, the term "sugar as used herein includes sugar derivatives such as amino sugars, oxidized and reduced sugars or esterified sugars. The above reaction may be carried out in a conventional manner analogously to the processes described in the Examples below, and if desired, protective groups suitable for peptides or sugars, protecting functional groups which do not participate in the reaction may be introduced into these reactions in these reactions. The term "protecting group" includes a polymeric resin containing functional groups. Compounds of formula I 'can be prepared by reacting a protected peptide containing a free amino group in a slightly acidic medium with a reducing mono-, di- or oligosaccharide or with the appropriate uronic acid or ester thereof (Amadori rearrangement), followed by deprotection. The reaction is carried out by a conventional method for the Amadori rearrangement. The acid to be added can be, for example, glacial acetic acid. When uronic acid is used in the reaction, additional acid may be dispersed therein. Preferably an excess of the hydrocarbon is used, e.g. 10 equivalents per one equivalent of the peptide. The reaction may be carried out in a polar solvent such as methanol, preferably at a temperature of about 60 to 70 ° C. Compounds of formula II can be prepared by reacting a protected peptide containing a free amino group in a weakly acidic environment with ketosis (Heyns rearrangement). The reaction can be carried out under the same conditions as the Amadori rearrangement (see above). Compounds of formula 3 can be prepared by reacting a protected peptide containing a free amino group with an acid of formula G3-COOH or a reactive derivative of such acid and removing the protecting group or groups. It may be a conventional amidation reaction which is carried out in a known manner. As reactive derivatives of carboxylic acids it is possible to use, in particular, acid halides. For example, amides can also be prepared from the free acids in the presence of hydroxybenzotriazole and dicyclohexylcarbodiimide. Compounds of formula 4a, 4b, 4c and 4d can be prepared by a) reacting the peptide first with a bridging member and then reacting the resulting product with sugar or b) reacting the sugar first with a bridging member and then reacting the glycosylated bridging member with a peptide. This reaction can be carried out in a conventional manner. Usually, amides, esters or acetals are obtained as the main products of the process according to the invention. The compounds according to the invention can be purified by a conventional method. Compounds of formula 4a in which Q is -CO- or -CS- can be prepared, for example, by coupling the appropriate glycosylisocyanate or glycosylisothiocyanate of general formula 23 as shown in the figure wherein L is O or S and G4 is as defined above and wherein the free hydroxyl groups present in G4 are protected, e.g. acylation, with the peptide P-NH2 in a protected form and subsequent deprotection of the protecting groups. This reaction can be carried out in a manner conventional for the production of swordfish derivatives. Compounds of formula 4c and 4d can be prepared by e.g. Amadori or Heyns rearrangement as described above in the preparation of compounds 1 and 2. 157 648 The compound of formula 5a or 5b can be prepared, for example, by a ') reductive amination of aldose, deoxyaldose or ketose with the peptide P-NH2- or b') reduction of the hemi-acetal group in the compound of formula 1 or 2, where appropriate reagents are used can be temporarily protected. Reductive amination and reduction can be carried out in a conventional manner. Reductive amination can be carried out with NaBHeCN, for example. The pH is preferably 7. The reduction of the hemi-acetal group can be accomplished with a borohydride, for example NaBH4, at a preferred pH of about 6. Starting materials, unless their preparation is described in detail, are known or can be prepared by a conventional method, e.g. A preferred group of compounds according to the invention comprises sugar derivatives of somatostatin, e.g. The term "somatostatin also includes analogs or derivatives thereof. Particularly preferred are the sugar derivatives of the compounds of formula 8 shown in the figure wherein A is hydrogen, alkyl of 1 to 3 carbon atoms or alkanoyl of 1 to 4 carbon atoms, the group> N-CH (Zi) -CO is 1) radical ( L) - or (D) -phenylalanine, optionally substituted with halogen, NO2, NH2, OH, alkyl with 1 to 3 carbon atoms and / or alkoxy with 1 to 3 carbon atoms or 2) radical of natural lipophilic α-amino acid or corresponding (D) -amino acid other than specified in item 1), where Z1 in the group> N-CH (Zi) -CO- is an amino acid radical as defined in items 1) and 2), A 'is hydrogen or alkyl containing 1 to 3 atoms carbon, Y1 and Y2 are each independently 1) hydrogen, 2) a group of formula 24 in which m is an integer from 1 to 4, R1 is CH3 or C2H5 and Rb is H, CH3 or C2H5 or 3) the group of formula 25 in which n is an integer from 1 to 5 or 4) a group -CO-NHRc in which Rc is a straight or branched alkyl radical from containing 1 to 6 carbon atoms or 5) a group of formula 26, in which Rd is a natural α-amino acid radical (including hydrogen) which is placed on the a-carbon atom, and Re is an alkyl radical containing 1 to 5 carbon atoms, 6) a group of formula 27, in which R ' _a and R'b, independently of each other, are hydrogen, CH3 or C2H5, Ra and R9 independently of each other are hydrogen, F, Cl, Br, alkyl containing 1 to 3 carbon atoms or alkoxy of 1 to 3 carbon atoms, p is 0 or 1, q is 0 or 1, and r is 0.1 or 2 or Y1 and Y2 together represent a bond, B is Phe, optionally substituted in the phenyl radical with F, Cl, Br , NO2, NH2, OH, alkyl of 1 to 3 carbon atoms or alkoxy of 1 to 3 carbon atoms, C is L- or D-Trp, optionally substituted in the benzene ring with F, Cl, Br, NO2, NH2, OH, alkyl of 1 to 3 carbon atoms or alkoxy of 1 to 3 carbon atoms, D is Lys, in which the α-amino group may be substituted with met ylem, F is Thr, Ser, Val, F is COOR1, CH2OR2, CO-NR3R4 or a group of formula 28, R1 is hydrogen or alkyl containing 1 to 3 carbon atoms, R2 is hydrogen or a radical of a physiologically acceptable, physiologically hydrolysable ester, R3 is hydrogen, alkyl of 1 to 3 carbon atoms, phenyl or phenylalkyl of 7 to 10 carbon atoms, but when R4 is -CH (Rs) -X and R3 is only hydrogen or methyl, R4 is hydrogen, alkyl of 1 to 3 carbon atoms or a group of formula 9, R5 represents a natural amino acid residue (including hydrogen) which is located on carbon a, or an OH-CH2- or -HO (-CH2) 3 radical, wherein the group of formula 9 may have the configuration L- or D-, Χ1 is COOR1, CH2OR2 or CO-NR6R7 where Re is hydrogen or alkyl of 1 to 3 carbon atoms, R7 is hydrogen, alkyl of 1 to 3 carbon atoms, phenyl or phenylalkyl of 7 to 10 carbon atoms, the radicals B, D and E are in the L form, and the radicals w positions 2 and 7, as well as the radicals Yi4) and Y24) exist independently in the D or L form, and salts and complexes of these compounds are preferred. Such compounds are disclosed in US Pat. No. 4,395,403. In the polypeptide derivatives of the above formula 8, the following meanings of the substituents and their combinations are preferred: If the group> N-CH (Zi) -CO- is as defined in p. 1), this radical is preferably (L) - or (D ) -phenylalanine or (L) - or (D) -tyrosine (wherein Z is benzyl or p-OH), especially the radical (D) -phenylalanine. If the> N-CH (Zi) -CO group is as defined in 2), radicals in which Z1 is an alkyl having 3, preferably 4 or more carbon atoms, e.g. up to 7 carbon atoms, are preferred. As the> N-CH (Zi) -CO- radical, the radical defined in item 1) is most preferred. 10 157 648 Υι and Υ2 are preferably as defined in 1, 2 or 4 above. They especially form a bond together. B is preferably Phe or Tyr, C is preferably - (D) -Trp, D is preferably Lys, E is preferably Thr, F is preferably a group of the formula CO-NR3R4, especially CO-NiRa / CH / Rsj-K :, in wherein the radical -CH (Rs) -Xi preferably has the L configuration. R3 is preferably hydrogen, R5 is CH2OH, CH (CH3) OH, i-butyl, CH2CH2OH or (CH2) 3-OH, especially CH2OH or CH (CH3) OH, especially CH (CH3) OH, Χ1 is preferably - CO-NReRz or CH2OR2, especially CH2OR2, R2 is preferably hydrogen. When R2 is an ester radical it is preferably HCO, an alkylcarbonyl of 2 to 12 carbon atoms, a phenylalkylcarbonyl of 8-12 carbon atoms or benzoyl. The radicals at position 2 and 7 preferably have the L configuration. Particularly preferred sugar derivatives of somatostatin are those having a sugar radical at the N-terminal amino group, e.g. compounds of formula 8a, 8b, 8c, 8d, 8e where O is CO or O) 8 and 8f. Compounds of formula 8a, 8b, 8e and 8f are particularly preferred. The group of compounds consists of compounds of formula 8pa, in which A ^p represents the radical of deoxyketose or a suitable uronic acid linked through a CH2 group with the NH group, the deoxy group being obtained by the reaction of Amadori aldose or the corresponding uric acid with a free amino group of somatostatin, and Z1, A ', Y1, B, C, D, E, Y2 are defined above in the definition of formula 8. Another group of compounds includes compounds of formula 8pb where G is the acyl radical of uranic acid, polyhydroxycyclohexanecarboxylic acid, N-acetyluraminic or N-acetyl-neuraminic acid, A is hydrogen, alkyl containing 1 to 3 carbon atoms or alkanoyl containing 1 to 4 atoms carbon, Z, A ', Y1, B, C, D, E, Y2, and F are as defined above. Suitably G is glucuronic, galacturonic or quinic acid. Another group of compounds are compounds of formula 8p _C , wherein Q is hydrogen or a glycosyl group of a mono-, di- or oligosaccharide, n is an integer from 1 to 6, A is hydrogen, an alkyl of 1 to 3 carbon atoms or an alkanoyl containing 1 up to 4 carbon atoms, Z, A ', Y1, B, C, D, E, Y2 and F are defined above. Compounds of formula I are preferably prepared by the process of the invention in which P is a group of formula 30, in which the meaning of the substituents is given in formula 8, and X in formula 1 is the deoxy radical of ketose or the corresponding uric acid, attached to the -NH- group via the group -CH2-, obtained by rearrangement of Amadori aldose or the corresponding uranic acid with the free amino group of the polypeptide radical of the compound of formula I or X is the acyl radical of uronic acid, polyhydroxycyclohexanecarboxylic acid, N-acetyluraminic or N-acetylneuraminic or X is the residue Qi- CCniHtania, where Qi is hydrogen or a glycosyl moiety of a mono-, di- or oligosaccharide and n1 is an integer of 1-6. A preferred group of compounds according to the invention are also sugar derivatives of calcitonin. The term "calcitonin" includes naturally occurring calcitonins (extracted from natural sources, from cell cultures, etc., or synthetically produced) and their derivatives and analogues. Natural calcitonins that can be used include human, salmon, eel, chicken, bovine, ovine, rat, or porcine calcitonin, especially human, salmon, chicken and eel calcitonin. Derivatives and analogs of these calcitonins include, in particular, the structure of natural calcitonin in which one or more amino acid residues have been replaced by one or more other amino acid radicals and / or the S-S- bridge has been replaced by an alkylene bridge and / or in which one or more amino acid radicals have been omitted. Calcitonin sugar derivatives of the general formula 10 in which R is H or RCO, the RCO group is an acyl radical of a carboxylic acid, Y1 is a radical located on the σ-C-atom of the σ-amino acid, Y2 is a radical located on a- are particularly preferred. Catome of the σ-amino acid, the group -CH2-SS-CH2-CH (NH2) -COOH, -CH2-SS-CH2-CH2-COOH, - (CH2) s-COOH or -CH2-S-Y3, Y3 is an alkyl containing 1 to 4 carbon atoms, benzyl optionally substituted with a methyl or methoxy radical or a CH3CONH-CH2- group, 157 648 o is an integer from 1 to 4, Ae is Thr or D-Thr, s is an integer from 3 to 5, Ae is an aminoacyl radical of a neutral lipophilic La-amino acid, A _a is an aminoacyl radical of a neutral, lipophilic L- or Da - amino acid and Zi is a polypeptide radical which is located at position 10 to 31 of natural calcitonin or a derivative or analog thereof, which exhibits hypocalcemic activity, the radicals 1 to 4 Y′i in formula 10, independently of each other, may be such alone or different, and all amino acid radicals except the aminoacyl radical Ae may be in the L or D configuration; salts and complexes of these compounds are also preferred. Such compounds are described in the examples of British Patent No. 2 18-4729 A. Zi in formula 10 is a peptide radical which can be present at positions 10 to 31 of various known calcitonins, e.g. human, salmon, eel, chicken, bovine, sheep, rat or porcine calcitonin, as well as derivatives and analogues of these calcitonins showing similar activity. Derivatives and analogues of these calcitonins are understood to be, in particular, natural calcitonins in which one or more amino acid radicals have been replaced by one or more other amino acid radicals or the -S-S- bridge has been replaced by an alkylene bridge, or in which one or more amino acid radicals have been omitted. These Zi peptide radicals typically include 22 amino acids, but may also contain correspondingly fewer amino acid radicals by omitting one or more amino acid radicals (des-aminoacyl derivatives). Zi is preferably a) Gly-Thr-Tyr-Thr-Gln-Asp-Phe-Asn-Lys-Phe-His-Thr-Phe-Pro-Gln-Thr-Als-Ile-Gly-ValGly-Als b) Gly-Lys-Leu-SerrGln-GIu-Leu-His-Lys-Leu-Gln-ThrrTyr-Pro-Arg-Thr-Asp-Ysl-Gly-AlaGly-Thr c) Gly-Lys-Leu-Ser-Gln-Glu-Leu-Hi - Ly - Leu-Gln-ThΓ-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Serr Gly-Thr Among the compounds of formula 10 in which Ζ _Ί is as defined in b) or c), those in which Zi is as defined in c) are preferred. RCO is preferably an acyl residue of an aliphatic, cycloaliphatic, aromatic or heterocyclic carboxylic acid. R preferably represents a ') saturated or unsaturated straight chain or branched alkyl having 1 to 17 carbon atoms, especially saturated alkyl having 3 to 9 carbon atoms, b') cycloalkyl having 5 to 7 carbon atoms or cycloalkylalkyl in which the cycloalkyl group contains 5 to 7 carbon atoms and the alkyl radical contains 1 to 2 carbon atoms, c ') adamantyl, adamantylmethyl or adamantylethyl or d') phenyl, benzyl or phenethyl. In the above-mentioned meanings of R, the alkyl, cycloalkyl or phenyl radicals may be substituted with the usual substituents, e.g., halogen, NO2, OH, alkoxy, etc. The RCO residue may, for example, be a σ-desaminated natural σ-amino acid residue. The meaning of R as defined in a '), b') and c ') is particularly preferred. ΥΊ and Y'2 denote radicals that occur on the σ-C-atom of the σ-amino acid, especially radicals that are bound to the σ-C-atom of the natural σ-amino acid, but may also denote the radicals of other σ-amino acids , e.g. 3-cyclohexylalanine or σ-aminoisobutyric acid. When o in formula 10 is the number 4, then a) the N-terminal aminoacyl radical (corresponding to the second amino acid radical in the natural calcitonin sequence) is preferably Ser, Gly or Ala, b) the second aminoacyl radical (corresponding to the third amino acid radical in the natural calcitonin sequence) is preferably Asn or Ser, c) a third amino acid radical (corresponding to the fourth amino acid radical in the natural calcitonin sequence (preferably being Leu, Asn, Ser, Phe, D-Leu or a cyclohexylalanine radical, d) the fourth aminoacyl radical (corresponding to the fifth amino acid radical in the natural calcitonin sequence) is preferably Ser or Ala. 157 648 When o in formula 10 is the number 3, the N-terminal, second and third amino acid radicals have the same preferred meanings as defined above, in the case where o = 4, in b). When o in formula 10 is the number 2, the N-terminal and the second amino acid radical have the same preferred meanings as defined above in the case where 0 = 4 in c) and d). When o in formula 10 is the number 1, the N-terminal and second amino acid radicals are preferably Ser or Ala. A ₆ is preferably Thr. The group -NH-CH (Y ^Z 2) CO, preferably is Cys, a cysteine derivative as defined above for Y * 2 or a neutral lipophilic σ-aminoacyl radical, especially Ala or another neutral lipophilic σ-aminoacyl radical, especially Ala, Ae preferably is The aminoacyl radical of a neutral lipophilic σ-amino acid, especially Val or Gly, Ag also preferably is the aminoacyl radical of a neutral lipophilic σ-amino acid, especially Leu or Phe. In compounds of formula 10, o is preferably 2 when R is H or RCO or especially o is 1 and R is RCO. All amino acid radicals preferably have the L configuration. Glycosylated calcitonins (including derivatives and analogs) are especially those in which the N-terminal amino group or one or more amino groups is glycosylated on one or more side chains, e.g. compounds of the formulas 1a, 1lb, 1 1c, 11d, 1le, 11f, wherein Cale is a natural calcitonin radical or a derivative or analog thereof linked to a sugar radical via an amino group at the N-terminus or in a side chain. The calcitonin derivative of formula 10 can be prepared by methods generally known for the synthesis of such polypeptides. Polypeptides of the above formula can be prepared, for example, as follows: a) at least one protecting group found on the protected polypeptide in the sequence represented by the formula or is removed b) two peptide units, each containing at least one amino acid or a derivative thereof, as described for formula 10 in protected or unprotected form are linked together by an amide bond, the peptide bond being formed so as to obtain the amino acid sequence specified Formula 10, optionally followed by step a) or c) the compound of formula 10 in which R is hydrogen, in protected or unprotected form, is reacted with an acid of formula RCOOH or with a reactive derivative of this acid, optionally followed by step a) or d) to prepare a compound of formula 10 wherein Y2 is CH2-SS-CH2CH (NH2) -COOH or CH2-SS-CH2-CH2-COOH, or reacting a compound of formula 12 in protected or unprotected form with the compound of formula 13, in which R10 is a group facilitating the formation of an SS- bridge from the S atom of the CH2SH group in the peptide of formula 12, Rn is hydrogen or an amino protecting group, R12 is OH or a carboxyl protecting group, and V is hydrogen or a group NH or a compound of formula 14, in protected or unprotected form, wherein R10 is as defined above, is reacted with a compound of formula 15, optionally followed by step a). If the preparation of the starting compounds is not described, then the compounds are known or can be made and purified by conventional methods. The final products of the formula 10 can be similarly purified by the usual method until they contain less than 5% polypeptides as by-products. The peptides used as starting compounds in processes a) and b) can similarly be produced in a solution or solid phase known in the art. Preparation of peptide units that contain an SS-CH2-CH2-CH2-COOH or CH2-SS-CH ₂ -CH (NH 2) -COOH as the radical Y'2 can be carried out analogously to the method described above in section. D). In the process according to point d), compounds of formula 13 or 14 are used in which R10 is a known radical which reacts with mercaptans to form an S-S- bond. R10 is especially S-alkyl, -S-COOalkyl, a group of formula 29 or S-SO3-. In these radicals, alkyl is especially lower alkyl having 1 to 4 carbon atoms. Introduction of these radicals to compounds containing free SH groups can be carried out analogously to the methods known in the chemistry of sulfur compounds. Another preferred class of compounds includes the group of LHRH antagonists. 157 648 Preferred compounds include sugar derivatives of compounds of formula 16, wherein Ri is H or an acyl group having 1 to 7 carbon atoms, Ai is D-Phe, optionally substituted on the phenyl ring by F, Cl, Br, NH2, CH3 or OCH3, especially ' at the 4-position, β-D-naphthylalanine, D-Trp, optionally substituted at the 5-position or 6-position by F, Cl, Br, NH2 or OCH3 and / or substituted at the 1-position by formyl or acetyl, proline, 3,4-dehydroproline or Dpyroglutamine , Bi is D-Phe, optionally substituted on the phenyl ring with F, Cl, Br, NH2, CH3 or CH3O, D-methylphenylalanine, optionally substituted at the 4-position with Cl or [beta] -D-naphthylalanine, Ci is D-Trp, optionally substituted at the 5-position or 6-position with F, Cl, Br, NH2 and / or OCH3 and / or at the 1-position by HCO or CH3CO, β-D-naphthylalanine, 3-D-pyridylalanine, D-Tyr or Phe optionally substituted with F , Cl, Br, NH2, CH3 or CH3O, Di is Ser, Fi is Tyr or phenylalanine, optionally substituted on the phenyl ring with Cl, Br, NH2, CH3 or CH3O, Fi is D-Phe, optionally substituted on the phenyl ring with F, Cl, Br, NH2, CH3 or CH3O, D-Trp, optionally substituted at the 5 or 6 position with F, Cl , Br, NH2 or CH3O and / or in position 1 via formyl or acetyl, D-Tyr, β-Dnaphthylalanine, D-Leu, D-Ile, D-Nle, D-Val, D-Ser (OtBu), D- Arg, optionally dialkylated with 1-6 carbon alkyl or 5-6 carbon cycloalkyl, D-homoarginine, optionally dialkylated with 1-6 carbon alkyl or 5-6 carbon cycloalkyl, D-His, D-His ( Bzl), D-Lys or D-Om, both optionally dialkylated with 1-6 carbon alkyl or 5-6 carbon cycloalkyl, D-Phe- (P-NH2) or α-ρ-aminocyclohexylalanine, G1 is Leu, Nleu, Nva, N-amethylleucine, Trp, Phe, Met or Tyr, Hi is Arg, Lys or Om, optionally substituted with 1-6 carbon alkyl or 5-6 carbon cycloalkyl, Ii is Pro, hy droxyproline or 3,4-dehydroproline and Ki is D-Ala. E1 and Fi can be replaced by other radicals if desired. Di and Ki, if desired, may be Cys which are linked by an S-S bridge. If desired, one of the residues Di and Ki is Asp or Glu and the other is Orn, diaminopropionic or diaminobutyric acid, with the residues Di and Ki being linked by an amide bridge. The preferred meanings are as follows: R1 = acetyl or formyl, A1 = D-Phe, D-Phe (p-Cl), J-D-naphthylalanine, 3,4-dehydroproline, Bi = D-Phe optionally substituted as indicated above, Ci = D -Trp, optionally substituted as indicated above, Di = Ser. Substitution with one substituent is preferred, (i) Fi - Tyr or Phe optionally substituted as indicated above when Fi - D-Phe or Lys or (ii) Fi = D-Phe or Lys when Fi - Tyr or Phe optionally substituted as indicated above, Gi = Leu, Hi = Arg, I = Pro, Ki = D-Ala. In the above-mentioned LHRH antagonists, the sugar residue is preferably linked to an N-terminal amino group or to a free amino group in the side chain. The sugar derivatives preferably have the structure given by the formulas 16a, 17, 18, 19, 20, 21, wherein NH-LHRH-Antag. represents an LHRH antagonist of formula 16. In Formulas 16a to 21, only one sugar group bound to the amino group is shown for simplicity. However, if desired, more than one sugar residue may be present in the compounds. Preferably there are two such sugar residues. The starting materials and the synthesis of unmodified LHRH antagonists are, for example, described in EPA 81 887 and 201 260 A. Further preferred polypeptides are: a) oxytocin and vasopressin as well as their derivatives, e.g. Lys ^{8 -} vasopressin and Orn ^{8 -} vasopressin, b) growth hormone releasing factor. The preparation of the starting compounds can be carried out in the liquid phase or by solid phase synthesis. The process of the invention preferably produces compounds of formula 1, wherein P is the residue of a biologically active peptide of formula NH2-P, where the NH group occupies a position at the N-terminus or side chain of the P polypeptide, X represents the group of formula 31, which is a reducing mono-, di- or oligosaccharide residue or the corresponding glucuronic acid or amino sugar, or X is a group of formula 32 which is linked to 157 648 through the -CH2 group with the -NH- group of the biologically active peptide deoxy radical of ketose or the corresponding uronic acid, resulting from the Amadorie rearrangement of aldose or the corresponding uronic acid with the free amino group of the polypeptide, or X is a group of formula 33, which is linked to via -CH2- with the group -NH- of the biologically active peptide deoxy radical of aldose resulting from Heyns rearrangement with a free amino group of the polypeptide, or X represents a group of formula G4-CO-, in which G4 is a uronic acid residue, a polyhydroximono- or dicarboxylic acid, or X represents groups of formula 34, 35 or 36, in which G6, G6, G'6 are sugar radicals and Q ', Q and Q' are groups linking the peptide radical with the sugar radical and acid addition salts and complexes of these derivatives, provided that 1) if in the above-mentioned compounds of formula I, X represents a group of formula 31 or G4-CO-, then P cannot be a radical of formula X-Pre-Phe-Phe-Y'-Z ' where X 'i Z 'stands for D-isomers of natural σ-amino acids, and Y stands for natural α-amino acid, 2'if in the above-mentioned compounds of formula 1, X represents a group of formula 32, then P cannot be a gastrin peptide radical, 3) if in compounds with formula I X represents a group of formula 34 in which Q is a group of formula -CH (CHe) Gln, then P cannot be a natural somatostatin radical. The compounds according to the invention have a pharmacological action and can therefore be used as pharmaceuticals for therapeutic purposes. The activity of the compounds of the invention can be observed in standard pharmaceutical and biopharmaceutical tests. These compounds, when administered orally or by injection, are usually at least as effective as unmodified peptides (e.g. the corresponding sugar-free peptides). They are usually better absorbed, more easily soluble in water and have a longer duration of action. The compounds according to the invention are therefore indicated for use under the same conditions as the unmodified peptides. The compounds of the invention can be compared to unmodified peptides in standard bioavailability tests. The compounds of the invention can be detected in the blood plasma for a longer period of time after administration than the unmodified peptides, as demonstrated by standard bioavailability tests. The compounds of the invention and the unmodified peptides can be administered, for example, to dogs in a single dose sufficient to achieve a therapeutic effect, either orally or intravenously. The doses used are at which the peptides or their metabolites are detectable in the blood. Detection may be carried out by a conventional method, e.g., by radioimmunoassay. In the above-mentioned test, for example, a 10-fold higher blood concentration of the compound produced by the method described in Example 2 below, given orally, was found compared to octreotide. The absolute bioavailability of the compound of Example 2, when administered orally and intravenously, as measured by AUC (area under the curve) is 5 times greater than that of octreotide. Elimination after intravenous administration is approximately 23 hours compared to approximately 0.5 hours for ocotide. Furthermore, the compounds of the present invention are conveniently excreted to a greater extent by the kidneys, which can be observed in standard tests. The starved male rats (225-375 g) were orally dosed with water (50 ml / kg). After 30 minutes, the animals were anesthetized with e.g. Inactin (100 kg / kg and p.). Cannulas were connected to the bile duct and bladder. Both jugular veins were exposed. One vein was infused with 5% glucose with 1% ethanol (5 ml / hr) to induce diuresis. The other vein was used to collect blood samples (0.5 ml) every hour for 4 hours. The compounds of the invention and unmodified peptides were administered subcutaneously at a dose of from about 10 to about 1000 micrograms / kg. The concentration of the compound was determined by a conventional method e.g. For example, the above test gave the following results for the compound of Example 2 and the unmodified H-DDPhe-Cys-Phe-Dtrp-Lys-Thr-Cys-Thr-ol (octreotide) peptide at a dose of 10 micrograms / kg: 157 648 The percentage of excretion by Bile Urine Compound according to example 2 1.6 36 Octreotide 22 19 While octreotide is excreted in both bile and urine, the compound of Example 2 is mainly excreted in the urine. The improved absorption of the compounds of the invention when administered orally can be determined as follows: The compound of the invention and the unmodified analog are orally administered to OFA rats (e.g. 10 mg / kg). After a specified period of time, e.g., 15.30 and 60 minutes, blood samples are taken and analyzed for drug content e.g. by the RIA technique. In this test, it was found, for example, that the compound of Example XLIV at a dose of 10 mg / kg showed 50 to 100% higher absorption than the unmodified oxytocin peptide. The results are as follows: Table Rat plasma levels after oral administration. The results are given in mg / ml 15 min. 30 minutes. 60 min. Oxytocin 7.33 3.00 2.55 Compound of Example XLIV 11.79 3.90 3.98 The pharmacological activity of the compounds of the invention can be tested in standard pharmacological tests, e.g. after injection, and if necessary compared with the activity of the unmodified peptides, e.g. in terms of effectiveness and duration of action. For example, pharmacological tests are carried out to test the effects of the compounds of the invention on hormones in animals. Compounds that inhibit hormone secretion can be tested by measuring the reduction in blood hormone levels. Compounds that inhibit GH (growth hormone) secretion, especially compounds of formula 8, especially compounds of formulas 8a through 8f, and reduce blood GH levels, can be tested as follows: Rhesus monkeys (at least 5) of the non-human primates were given a compound according to the invention in a banana piece as a carrier. The compound was administered at a dose of from about 0.1 mg / kg to about 10 mg / kg orally. Blood was drawn from V. Saphen through a catheter. The blood GH concentration was measured by RIA (radioimmunoassay). For example, in this test with rhesus monkeys, the compound of Example 2 at a dose of 0.1 mg / kg reduced GH secretion by at least 50% over a period of more than 10 hours, compared to a 5 hour depletion period caused by unchanged peptide - octreotide. Another test was performed as follows. Male rats were decapitated and blood was collected 1 hour after administration of a GH secretion inhibiting compound in several logarithmically staggered doses. Serum GH levels were determined by the RIA technique. In this test, the compounds of the invention are active at doses from about 0.02 to about 30 micrograms / kg, administered subcutaneously. This test has determined, for example, that the compounds of Examples I, II, XXI and XXIV, administered subcutaneously, exhibit the following ID50 values: 0.045.0.190.0.3 and 0.2 micrograms / kg respectively compared to ID ₅ for natural somatostatin obtained in the same test, administered subcutaneously at a dose of 93 micrograms / kg (the ID50 represents the amount of compound needed to reduce the GH content by 50% compared to the level in control animals that were not administered the test compounds). Unlike natural somatostatin, the GH-inhibiting compounds of the present invention are still highly active in this test over a long period of time (e.g. 6 hours). The GH-reducing effect of these compounds was also observed after oral administration 157,648 was administered to male rats implanted with estradiol. Relatively small changes in GH levels were observed in this test. The test was performed as follows: A loop (50 mm in length and 3 mm in diameter) of silastic containing 50 mg of estradiol was implanted under the dorsal skin of male rats weighing approximately 300 g, dormant with ether. At various time intervals (1 to 6 months later) these animals were reused for testing. The test substance was administered either subcutaneously or orally. About 0.8 ml of blood was collected from the retroorbital plexus immediately through and at various time intervals after the administration of the substance. The blood was centrifuged and the plasma level of GH was determined by radioimmunoassay. The orally administered compounds of the invention are more active than the corresponding unmodified peptides, even after several hours. The ID50 for each of the compounds of Examples I and II is about 17 to 40 times lower than the ID50 of the unmodified octreotide peptide. The following results were obtained: Compound of the Example ID 50: o. Micrograms / kg XXI 500 XXIV 25 Octreotide 1400 The compounds of the invention are therefore indicated for use in the treatment of diseases where it is desired to inhibit GH secretion. The main indications include diabetes mellitus, prevention and treatment of vasculitis and proliferative retinal degeneration, as well as acromegaly. Compounds of the invention that inhibit GH secretion also inhibit pancreatin secretion, which can be detected in animal tests. The method described in Scand can be used. J. Gastroint. 6, 423 (1975) by S. J. Konturek's et al. The compounds of the present invention that inhibit GH secretion also inhibit gastric acid secretion and gastric pH. The activity of these compounds is observed, for example, in the following test: Gastric fistula rats are fed via a gastric tube with GH secretion inhibiting compounds of the invention at a dose of from about 0.05 mg / kg to about 5 mg / kg. After 1 hour, the fistula was opened. Gastric juice was collected within 30 minutes. The volume of collected juice was recorded and the acid concentration was determined. In the above-described test, the compound of Example 2 increased the pH to 6-8 over 3.5 hours. Octreotide increased the pH to 6-7 for only 2 hours. The compound of Example 2 is at least 60 times more active than cimetidine in this test. The compounds according to the invention which inhibit GH secretion, in particular the compounds of formula 8, are therefore indicated for use in the treatment of gastrointestinal disorders, e.g. for the treatment of peptic ulcers, gastrointestinal hemorrhages, acute pancreatitis and gastrointestinal-pancreatic tumors. (eg, islanders, "vipomas" tumors, "glucagonomas" etc). The compounds according to the invention inhibit GH secretion, also inhibit the proliferation and / or keratinization of epidermal cells and are therefore indicated for use in the treatment of dermatological diseases which are associated with pathological proliferation and / or keratinization of epidermal cells, especially in the treatment of psoriasis. Furthermore, these compounds are intended for the treatment of senile degenerative dementia, also of the Alzheimer's type (SDAT) or for the treatment of recurring headaches. In all of these uses, an indicated daily dose is from about 2 micrograms to 20 milligrams of GH secretion-inhibiting compounds according to the invention. The compounds can be administered in divided doses 2 to 4 times a day in unit doses or in sustained release form as needed. Such unit doses may contain from about 0.5 micrograms to 10 mg. The sugar derivatives of calcitonin and calcitonin analogs or derivatives according to the invention, in particular the derivatives of formula 10, reduce plasma calcium levels. 157 648 Moreover, they are functional antagonists of parathyroid hormone and have a beneficial effect on the calcium balance in the bones. The hypocalcemic activity of these compounds can be measured in a known manner, e.g. according to the method of M. Azria et al. presented in Calcitonin 1984 Symposium, October 24, Milan and published as "Short Communication *" in "Current Clinical Practice Series" No. 43. Excerpts Medics 1986, 104. This method used a selective Ca ²⁺ electrode, making it possible to measure continuously the calcium ion content in the blood of young rabbits or dogs. The compounds were administered intravenously at a dose from about 0.1 to about 10 micrograms / kg, e.g. adjusting to about 1 international unit per kg. Measurements were carried out for 5 hours and the AUC "area under the curve * ¹ " was calculated. Compounds can also be tested in other tests, e.g. in the hypocalcemic standard tests of M. Kumare et al., J. Endocrinology (1965), 33, p. 469, in rats at various doses of compounds exhibiting a hypocalcemic activity of 300 to 600 international units per year. mg of hypocalcemic compounds according to the invention. For example, it has been found that the compounds of Examples XXXVII and XXVIII, when administered intravenously to dogs at a dose of 5 mg / kg, show activity over a much longer period than the unmodified peptide. In this test, a 15 to 18% reduction in blood calcium was observed for Compounds C and D after 3 hours; after 6 hours, the reduction in calcium by the unmodified peptide was not detectable, while the reduction in calcium by the compounds of Examples XXXVII and XXXVIII was still at 3 hours. The hypocalcemic compounds according to the invention are therefore indicated for use in all cases where a reduction in plasma calcium or an effect on bone metabolism is desired, e.g. hypercalcemia due to a lack of endogenous thyrocalcitonin due to loss of thyroid tissue or hyperparathyroidism. They are also indicated in all cases of bone diseases in which there is an increased tendency to fracture or in which calcium retention in the bones is desirable, e.g. ossification of all types of bones (e.g. post-climacteric, post-traumatic, caused by treatment with corticosteroids or inactivation, by malignant diseases). etc.), fracture, bone softening, abnormal bone development due to rickets and kidney disease, pain, e.g. bone pain due to sagging, degenerative nerve disease, Paget's disease and in combination with calcium phosphate treatment. For the above lime applications, the indicated daily dose is from about 5 to about 1500 International Units, and may be administered as one dose per day or every 2 to 3 days as needed. Compounds of the invention which are sugar derivatives of LHRH or analogs thereof inhibit the secretion of luteinizing hormone, e.g. as shown by inhibition of ovulation in animals. The test was carried out according to M. Marko and F. Fluckiger, Experientia 30, 1174-1176 (1974). Adult female rats of the Ivanovas Wistar strain (Sprague Dawley; Iva: SDIV, 200-250 g) were kept under standard conditions: 14 hours light (4 to 18 hours), 24 ° C, 55-60% RH, food and water ad libitum. Animals with a 4-day regular cycle were either subcutaneously injected or orally dosed with the test compound at the peak of the estrogenic phase at 13.00 hours. The next day, at 9 am, the rats were sacrificed and the eggs were counted on both Falloppia tubes using a dissecting microscope. Only when no egg was found was ovulation considered to be inhibited. The mean number of eggs per ovulating rat in each test group was also determined. Generally, these compounds of the invention are effective in the range of from about 0.0005 to about 10 mg / kg. For example, the compound of Example XLV is active at a dose of 0.01 mg / kg, p. C. The luteinizing hormone secretion-inhibiting activity of the compounds according to the invention was also tested in another in vitro test: Pituitary cell cultures were prepared according to the method of Vale (W. Vale and G. Grant: Methodes in Enzymology 37, 82-93 (1975) as previously described (M. Marko and D. Romer: Life Sciences, 33, 233-240). / 1983 /). Primary cultures were kept for 4 days in incubation at 37 ° C. 157 648 The cells were then washed and incubated for 3 hours in 1 ml of LHRH or test compound containing medium. At the end of the incubation, the supernatant was removed and LH determined by a LH-specific radioimmunoassay. In this assay, it was found that the normally tested compounds are effective in inhibiting secretion induced by LH LHRH in a dose-dependent manner in a concentration range of approximately 10 1 ^{_ 2} to about 10 ^"7 M. For all LHRH applications, an indicated daily dose of the compounds of the invention is in the range of about 2 micrograms to 20 mg of the compound. If necessary, the compounds can be administered in divided doses 2 to 4 times a day in the form of a unit dose or, if necessary, in a sustained-release form. Such unit doses may contain from about 0.5 micrograms to 10 mg. For example, for the compound of Example 2, the indicated dose is 3 to 10 mg three times a day, e.g. orally for ulcers or diabetics or for the treatment of acromegaly. The compounds of the invention may be administered by any method, e.g. enterally, e.g. orally, e.g. in the form of drinking solutions, tablets or capsules, nasally, e.g. in the form of powders or liquids as aerosols and ointments, or parenterally, e.g. injection solutions or suspensions. Appropriate dosages of the compounds of the invention by a particular mode of administration, e.g. nasal or oral administration, can be determined by bioavailability tests in which the same substance is injected intravenously, intramuscularly or subcutaneously. Typically, daily doses for oral administration are about 10 to 100 times higher than doses suitable for intravenous or subcutaneous injection. The compounds of the invention may be administered in any pharmaceutically acceptable form, e.g. in free form, e.g. in free base form or, when the compound is an acid, in free acid or pharmaceutically acceptable salt form. For example, the salt can be an acid addition salt or, when the compound is an acid, a pharmaceutically acceptable cationic salt. The compounds can also be administered as a complex. The compounds may additionally or alternatively be in the form of a solvate, e.g. a hydrate. The compounds according to the invention exhibit the same activity in each of these forms. The compounds of the invention can be prepared into pharmaceutical compositions together with at least one pharmaceutical carrier or diluent together with at least one pharmaceutical carrier or diluent. The solution in drinking or injection ampoules may contain 0.5 mg per ml of the compound of Example 2 in the form of acetate, 11.45 mg of citric acid, 6.32 mg of NaOH, 4.5 mg of NaCl. The compounds of the present invention have the above-indicated use, which includes the reduction of GH secretion, the treatment of diabetes mellitus, the reduction of gastric secretion, and the treatment of acromegaly by somatostatin-like compounds. In the examples below, all temperatures are given in degrees Celsius and the uncorrected values of [σ] ² ° ο · The following abbreviations are used: AcOH = acetic acid; Boc = tert-butyloxycarbonyl; But = tert-butyl; DCCi = dicyclohexylcarbodiimide; DMF = dimethylformamide; Fmoc = 9-fluorenylmethoxycarbonyl; MeOH = methanol; NEt3 = triethylamine; Thr-ol = the threoninol radical - CH3-CHOH-CH (CH2OH) -NH-; TFA = trifluoroacetic acid; HOBT = hydroxybenzotriazole; hpGRF = human pancreatic growth hormone releasing factor; HOSu = N-hydroxysuccinic acid imide. All peptides were obtained as polyacetate polyhydrate with a peptide content of 70 to 90%. Analysis by pressure liquid chromatography showed that the peptides contain less than 5% of other peptides. The factor "F" mentioned in the following examples determines the peptide content of the products obtained (F = 1 corresponds to 100% peptide content). The difference to 100% includes acetic acid and water [(1-F) X 100], All sugars have the? Configuration, unless otherwise specified. Deoxy = deoxy. Example I. Preparation of N ^ff - /! - deoxyfructosyl-DPhe-Cys-Phe-DTrp-Lys-Thr-s-Thr-ol acetate of formula 37. a) H-Phe-Cys-Phe-DTrp-Lys (Boc) -Thr-Cys-Thr-ol 157 648 2.25 g of di-tert-butyl percarbonate, dissolved in 30 ml of dimethylformamide, was slowly added dropwise at room temperature to a solution of 10 g of H-DPhe-Cys-Phe-DTrpLys-Thr-Cys-Thr-ol acetate in 100 ml of dimethylformamide. After two hours at room temperature, the solvent was removed in vacuo and 200 ml of diisopropyl ether were added to the residue. The resulting precipitate was filtered off, washed with diisopropyl ether and dried. The crude product was purified by chromatography over silica gel (eluent: CH 2 Cl 2 (MeOH 9/1) and isolated as a white amorphous powder, [a] d: 29.8 ° (c = 1.28 in dimethylformamide). b) N ^ff - / l-Deoxyfructosyl-DPhe-C! ys-Phe-DTrp-Lys (Boc) -Thr-Cys-Thr-ol 2 g of D- (+) -glucose and 0.5 g of the final product from step a) were dissolved in 20 ml of MeOH / OHAc 9/1 (v / v) and kept at 60-70 ° C for three hours. After concentration by evaporation, a small amount of methanol was added to the product and the title compound was precipitated with diisopropyl ether, followed by chromatographic purification over silica gel (eluent CHaCk / MeOH 9/1). An amorphous white powder was obtained. [σ] ² %: 12.0 ° (c = 1.04 in DMF). _Λ c) To 400 mg of (N ^a - /! - deoxyfructosoyD-Phe-Cys-Phe-DTrp-Lys) (Boc) -Thr-Cys-Thr-oiu 3 ml of trifluoroacetic acid 100% was added and kept at room temperature until until the starting compound is completely dissolved (5 minutes). After adding 20 ml of diisopropyl ether, the title compound precipitated, which was then filtered off and washed with diisopropyl ether. The title compound was purified by chromatography over silica gel (eleuent: CHCl3 (MeOH / HOAc) H2O7 / 3 (0.5 / 0.5 / 0.5) and isolated as a white lyophilisate. [Ct] ²⁰ d: -31.3 ° (c = 0.52 in HOAc 95%) F: 0.88. Example II. Preparation of Ng-te-glucosylU- [beta] -deoxyfructosyl-SMS of Formula 38 wherein SMS is the peptide radical -DPhe-Chys-Phc-DTrp-Lys-Thr-Cys-Thr-ol. The title compound was obtained as acetate by the procedure described in Example 1, starting with D (+) -maltose instead of D-glucose; [α] 2 ° -: -7.9 ° (c = 0.71 in 95% AcOH) F: 0.91. Example lll. Preparation of the Nf ^r - (< 7-glucose / 1-4) -cr-glucosyl / 1-4 / - / 1-deoxyfructosyl] SMS of Formula 39 where SMS is as defined above. By the method described in Example 1, the title compound was obtained in the form of an acetate instead of D-glucose from maltotriose; [σ] 2 ° ₀ = + 11.3 ° (c = 0.71 in 95% AcOH), F: 0.78. Example lV. Preparation of N ^α -Fructofuranuronic acid-SMS of Formula 40, wherein SMS is as defined above. The title compound was obtained in the form of an acetate using the procedure described in Example 1, starting from D-glucuronic acid instead of D-glucose; [ct] ² ° d = -29.4 ° (c = 0.34 in 95% AcOH) F: °, 88. Example 5 Ng-deoxysorbosyl-SMS of Formula 41 wherein SMS is the radical as defined above. The title compound was obtained in the form of an acetate by the method described in Example 1, starting with D (+) -galactose instead of D-glucose; [σ] 2% = -30.4 ° (c = 0.50 in 95% AcOH), F: 0.85. Example Vl. ^Cr N - [Ol / 3-D-glucosyl (l-4) SMS--deoksvfruktozyio of formula 42, wherein SMS is as defined above. Following the procedure described in Example 1, the title compound was obtained as an acetate starting from D (+) -celebiosis; [σ] 2% = -28.1 ° (c = 0.47 in 95% AcOH), F: 0.81. Example VII. N-α-L -deoxyfructosyl-SMS of Formula 43, wherein SMS is as defined above. Following the procedure described in Example 1, starting with L (-) - glucose instead of D- (+) -glucose the title compound was obtained as an acetate; [a] 2 ° D = -20 ° (c = 0.46 in 95% AcOH), F: 0.91. Example VIII. N ^α - [O- (3-D-glucosyl-l- [beta]] -deoxyfructosyl-SMS of Formula 44, wherein SMS is as defined above. By the method described in Example 1, the title compound was obtained in the form of acetate instead of D-glucose, starting from gentiobiosis; [ct] ²⁰ d = 23.5 ° (c = 0.46 in 95% AcOH), F: 0.76. Example lX. N ^σ - [O - /} - D-galactosyl- (i-4) -deoxvfructozyi -)] - SMS of the formula 45, wherein SMS has the above meaning. 157 648 Using the procedure described in Example I, starting from D (+) -laktozy instead of D-glucose to give a compound t in ^s tułowy ^{p stand} to ethyl; [σ] ²⁰ = -29 ^{°, 3} ° (c = ^90.55, 95% AcOH ^ F: ^0, 83. Example 10 N- (O-α-galactosyl- (1-6) -deoxyfructosyl-SMS of formula 46. Using the procedure described in Example I, starting from melibiose instead of D-glucose was obtained from the related ^{± c t} tufc> ^y in the ^p ostaci ^acetate; [σ] ² °° - 8, ⁴ ° (c = ^0.5 in ^95% AcOH ^ F: ^{0.76. p} rz ^yk order ^{χ Ι.} [N- (1-deoxy- ^D - ^f ru ^k toz ^yl o) -Tyr ³ ] - ^SMS of the formula ⁴ 7. Salmon ^{sp b} I O ^{p p} m isan ^y y ^{y k} counter and, starting from ^{Tyr 3} - ^{SMS text message} instead will wipe ^y mano zwózek tytutowy in the acetate ^form; [σ] ² %> = - ^32.2 ° (c = ^0.9 in ⁹⁵ % AcO ^H ), F: ^0.87 . ^p rz ^yk order ^{χ Η. [N} - (cr-D-gIukopiranozylo - L ⁴⁾ - ^d EOL y ^^ ^ fi ^ i ^ ^ łktoz yl) ^ T r ^{s 3]} - S ^SM of formula ^48. The title compound was obtained as acetate by the method described in Example 1 starting with D (+) -maltose instead of D-glucose and with Tyr3-SMS instead of SMS; [0 (] ²⁰ D = -4.7 ° (c = 1.0 in 95% AcOH), F: 0.81. Example XIII. By the method described in Example 1, the compound of formula 49 was prepared by starting from D-gluccoheptose instead of D-glucose; [c, d = -12.9 ° (c = 1.0 in 95% AcOH), F: 0.91. Example XIV. By the method described in Example 1, starting from D (+) -glucose and SMS in which the -NH2 group of lysine is unprotected, the compound of formula ^{50 was} obtained in which ^y m R is ^g roup of formula ^1; [α] = ^2% - ^42.4 ° (c - ^{0.37, 95%} Ac ^OH X ^{F: 0,} 83. Example XV. Using the procedure described 'in Example I, starting from glukoheptozę and SMS, wherein the -NH2 group of lysine is unprotected, to give a compound of formula ^{52 wherein R} ru ^{g PE} of formula ^{53 in} the ^p ostaci ^acetate; [α] ² % = - ^9.3 ° (c = ^0.41 in ⁹⁵ % AcOH), F: 0.84. Example XVI. Fructosyl-6-phosphate-SMS of formula 54. Using the procedure described in Example I, starting from compound D-glucose-6-phosphate, ^D-gl zairnast ukozy ^± relationship related to afford the title acetate ^form; [σ] ² % - - ^19.5 ° (c = ^1.0 in ⁹⁵ % AcOH), F: 0.89. Example XVII. Using the procedure described in Example I, starting from compound ^D -ryboz ^that instead of D-glucose will wipe ^{y y} mano compound of formula ^55; [σ] ² % = - ^{3 1.8} ° (c = 1.0 ^{in 95} % AcOH). Example XVIII. N ^G -deoxy-fructosyl- (D) Phe-Cys [<COC - ((CH3) 3] -Phe- (lD) -Trp-Lys-ThrCys [[COC (CH3) 3] -Thr-ol _t _, a) Deoxyfructosyl- (D) ^p he-Cys-Phe - D) Trp-Lys (COC) -Thr-Cys-Thr-ol. 0.58 g of the compound prepared as described in Example 1 in 10 ml of DMF was mixed with 0.08 ml of NFt3 and then with 0.12 ml of (BOC) 2O. The mixture was stirred for about 15 hours at room temperature, concentrated in vacuo and stirred with ether. The precipitated product was filtered off. The residue was dissolved in a small amount of MeOH and the product precipitated by adding water. The product was filtered off, washed with a little water and dried to provide the title compound. [σ] ²⁰ = + 14.5 ° ^(c = ⁰ 7 DMF). b) Na-deoxyfructosyl- (D) -Phe'-Cys-Phe - D) Trp-Lys- (BoC) -Thr-Cys-Thr-ol. 0.51 g of the final compound from step a) in a mixture of 10 ml of dioxane and 2 ml of NFt3 (AcOH buffered to pH 8.6 under argon) was mixed with 0.4 g of dithioerythritol. The mixture was stirred for about 15 hours at room temperature and concentrated under argon. vacuo. the precipitated product was centrifuged. the residue was washed with a little water, then dried in vacuo. ^Ot y ^{y y} mano zwózek ^tytutów; [a] ² D = + ^3.8 (c = ^0.8 in ^DM F). c) NCf-deoxyfructosyl- (D) Phe'-Cys- [COC (CH3) 3] -Phe- (D) Trp-Lys (BOC) -Thr-Cys- [COC- (CH3) 3] -Thr-ol . 0.38 g of the final compound from step b) was dissolved under argon in 25 ml of N-methylpyrrolidone, then stirred at 0 ° C with 0.3 ml of N-methylmorpholine and 0.31 ml of pivaloyl chloride and further stirred for about 16 hours in 0 ° C. The product was mixed with diethyl ether and diisopropyl ether. The precipitated product was centrifuged. The residue was dissolved in a small amount of DMF and the product precipitated by adding MeOH and H2O. The product was centrifuged. The residue was dried in vacuo and used in the next step without further purification. d) N ^<a - ^d eoksy ruktozy ^{f l} o ^{(D) P} he- ys- ^C [C ^{OC (CH3)} 3] -Phe- (D) Trp-L ^{s s-Thr-C} ys ^[CO C ( ^CH 3) ³ ] Thr-ol. The residue from step c) was dissolved in 5 ml of TFA / H 2 O (9: 1) at 0 ° C and stirred for 15 minutes. The product was precipitated by adding ether (10% 5N HCl) ether. The product is purified by chromatography on silica gel in CHCl3 (MeOH / AcOH - H2O). 157 648 The fractions that contained the desired product were combined, concentrated in vacuo while adding water and then lyophilized. The title compound was obtained; [a] d = -15.3 (c = 1.0 in 95% AcOH), F: 0.88. ___ Example XIX. 2 - [(D) Phe-Cys-Phe- (D) Trp-Lys-Thr-Cys-Thr-ol [-2-deoxy-D-glucose of formula 56. And 'V 2 g D (-) fructose and 1 g H- (D) -Phe-Cys-Phe- (D) Trp-Lys (Boc) -Thr-Cys-Thr-ol (prepared as described in Example 1 step a) ( dissolved in 100 ml of MeOH / HOAc 9/1) and kept at 65 ° C for 16 hours. After concentration by evaporation, the product was dissolved in a little methanol and the crude product was precipitated with diisopropyl ether. The crude product thus obtained was subjected to cleavage of the protecting group (elimination of jOC) without further purification. 1 g of the obtained crude product was mixed with 20 ml of trifluoroacetic acid (100%) and kept at room temperature until complete dissolution of the starting compound (5 minutes). The title compound was precipitated by the addition of 200 ml of diisopropyl ether, filtered and washed with diisopropyl ether. Purified by chromatography over silica gel (eluent: CHCl3 (MeOH / HOAc) HzO 7/3 / 0.5 / 0.5) and isolated as a white lyophilisate; [σ] ²⁰ ο = -6.7 ° (c = 0.3 in HOAc 95%) F: 0.73. A second product can also be obtained which is a mixture of the 1: 1 isomers of formula 57 and 58 exhibiting an inverted configuration at the C2-carbon of the hydrocarbon group. Example XX. 2- [Tyr ³ -SMS] -3-deoxy-D-glucose of formula 59. By a method analogous to that described in Example 19, starting with Tyr ³ SMS instead of SMS, the title compound, F: 0.95, was obtained. __ _{_} Example XXI. Glucuronic acid amide and H-DPhe-Cys-Phe-DTrp-Lys-Thr-Cys-Throl of formula 60., 170 mg of glucuronic acid amide and H-DPhe-Cys-Phe-Lys- (BOC) -Thr-Cys-Thr-ol were treated with 3 ml of 100% trifluoroacetic acid until complete dissolution (5 minutes). The title compound was then precipitated as trifluoroacetate by the addition of 20 ml of diisopropyl ether, then filtered, dried and chromatographed on silica gel (eluent: CHCl3 (MeOH / HOAc) H2O 7/3 / 0.5 / 0.5) and the title compound was isolated in pure form as a white lyophilisate (acetate); [GT] ^20D - -2.9 ° (c = 1.0 in 95% AcOH); [ct] ²⁰ d - -29.2 ° (c = 0.48 in 95% HOAc), F: 0.85. The starting compound can be produced by the following method: (_ A solution of 135 mg POCI in 2 ml DMF was added to the DMF solution 450 mg H-DPhe-Cys-PheD ^T r ^p -Ly ^s ( ^B o ^c ) - ^Th r ^-C ys-'y ^h ro ^| u ^{, 117} m ^gk wasu ^g hicuronic ^g o ^{and 135} mg ^{HOBT, chilled} to -30 ° C. After 48 hours, with simultaneous thawing at room temperature, the resulting dicyclohexylurea is filtered off and the desired compound is precipitated by adding 20 ml of diisopropyl ether. The desired compound was isolated in pure form after filtration, drying and chromatography over silica gel (elunet: CH2Cl2- (MeOH 9/1); [fr] 2 ° p = -16.7 ° (c = 0.50 in DMF). Example XXII. Quinic acid amide and H-Dphe-Cys-Phe-DT rp-Lys-Thr-Cys-Thr-ol of formula 61.. The title compound was prepared as described in Example 21 starting from L (-) - quinic acid; [ff] 2O _D = -50 ° (c = 0.44 in 95% AcOH), F: 0.97._i Example XXIII. Sialic acid amide and H-DPhe-Cys-Phe-DTrp-Lys-Thr-Cys-Thr-plu of formula 62. The title compound was obtained by the method described in Example 21 starting from sialic acid; [σ] 2% = -60.8 ° (c = 0.6 in 95% acOH), F: 0.95. _t _, Example XXIV. N ^ff -O- (JD-glucosyl-oxyacetyl) -DPhe-Cys-Phe-DTrp-Lys-Thr-CysThr-ol of formula 63, _250 mg (tetra-O-acelyl-O- / 3-D- glucosyl) -oxyacetyl-DPhe-Cys-Phe-DTrp-Lys- (BOC) Thr-Cys-Thr-ol was dissolved in 10 ml of methanol and the pH was adjusted to 10 with a few drops of IN NaOCH3 in methanol. After about 15 minutes of reaction, the solution was neutralized with an ion exchange resin (eg AMBERLYST "15 H +) and the ion exchange resin was filtered off. The filtrate was concentrated and the residue was treated with 3 mL of trifluoroacetic acid for 5 minutes. The title compound was precipitated as trifluoroacetate by adding 20 ml of diisopropyl ether and isolated pure as a white lyophilisate after filtration, drying and chromatography on 157,648 silica gel (eleuent: CHCl3 (MeOH) -HOAc / H2O 7/3 / 0.5 / 0.5); [ct] ²⁰ d = -39.2 ° (c = 0.60 in 95% HOAc), F: 0.91. The starting compound can be prepared as follows: a) tetra-O-acetyl- β-D-glucosylglycolic acid benzyl ester. 2.5 g of 4A molecular sieves in powder form were added to a solution of 830 mg glycolic acid benzyl ester in 50 ml CH2Cl2 and after the addition of 2.8 silver trifluoromethanesulfonate a solution of 4.1 g acetobromoglucose in 50 ml CH2Cl2 was added dropwise. After 15 minutes, the reaction was quenched with 4 ml of pyridine, the solids were filtered off, and the filtrate was shaken with a 10% NaHSOi solution. After silica gel chromatography the title compound was isolated in pure ^p Ostade (eluent ^D chromatograph ^C H ₂ ^C l2 / Me ^OH 99/0; [a] o = ^M - ^22.4 ° (c = ^1.7 C ^H C3). b) tetra-O-acetyl-O-) - D-glucosylglycolic acid. 800 mg of tetra-O-acetyl-O3-D-glucosylglycoic acid benzyl ester was dissolved with 400 g of ethanol / water 1/1 (v / v / v) and mixed with 400 g of palladium on 10% activated carbon. After hydrogenation in the apparatus "PARR-APPA-RATUS: at 50 psi, the title compound was obtained, which was isolated in a crystalline form after filtration and concentration in vacuo; [a]% = 35.5 ° (c = 1.03 in MeOH). ____ c) ^Nc - ^{(t *} -acetyl etra- ° ^l ° o - / 3-glu eskers ^{k * l O-yl} oksyacet o) ^Ph e C ^f D ys-H2-D-Trp-Lys (B ^O C) -T ^h rCys-T ^h e-ol. . To a solution of 81 g of tetrα-O-ocetyl-O-O-Z-D-glucose glycolic acid. 225 mg of H-Dphe-CysPhe-DTrp-Lys (BOC) -Thr-Cys-Thr-ol and 45 mg of HOBT in 2 ml of DMF, chilled to -30 ° C, 45 mg of DCCl, dissolved in 1 ml of DMF, were added. After 48 hours and after thawing to room temperature, the dicyclohexylurea formed is filtered off and the title compound is precipitated from the filtrate by adding 20 ml of diisophenyl ether. ^I n ^k d la XXV. Opnsanym certain issues in Example ^IV to give XX ^N ° - ^(O - / 3-D-galactose revived ^t-oxyacetyl) -SMS of formula 64; [cr] d = -37.5 ° (c = 1 in 95% AcOH), F: 0.95. PrzyHad ^XXVI · ^{S pc-b} of the ^p -m opnsanym ^yk y ^ ^d ^ e ^XXIV will wipe ^y mano ^NFF - ^(O - / 3-ceIo ^bi-ozylc oksyac th ^l o) - ^SMS of formula ^65; [σ] ² % = - ^32.5 ° (c = l in ⁹⁵ % Ac ^OH X ^F : ^0.9 L Example XXVII. The method described in Example 24 gave N ^ff - (O- / 3- (O) glu2ozylc-o2-isobutyryl) -SMS of formula 66; [ar] ² d = -32.9 ° (c = 1 in 95% AcOH), F: 0.93. Example XXVIII. The method described in the example XXIV gave Ν ^σ - (Ο-α- (Ο) g ^^ zyto-a-jLj-oxyizowaier ^ doJ-SiMS! Of formula ^67; [σ] ² % ^{= 4} W, 3 ° (c = ¹ in ⁹⁵ % Ac ^OH X ^F : 1.0 °. Example XXIX. Using the procedure described in Example XXIV was obtained [N-Ac-tylomuranylc (DjPh / j-sms of formula 68, [ar] ² = ^-15%, 4 ° ^(c = ^{0 13, 95%} AcOH ^ ^{F: 0,} 9. Example XXX. [3-D-glucosyl-tickαrbαmoyl-O-αcetyIo-] / 3-D-glucosisoticcyαnion and the mixture was kept at room temperature for 1 hour. The mixture was evaporated in vacuo, a small amount of methanol was added to the residue and treated with diisopropyl ether, whereupon the product practically pure precipitated. To graft the Fmoc group and the acyl group, the product in 50 ml of absolute methanol was treated with a catalytic amount of IN NoOCH- in methanol. After 30 minutes, the reaction was complete (as judged by thin layer chromatography). The mixture was neutralized with 1% acetic acid and evaporated in vacuo. Water was added to the residue, followed by extraction with ethyl acetate. The aqueous phase was lyophilized. The residue was purified on silica gel and the reference was removed, for example, using Duokite. The title compound was obtained as a lyophilisate; [α] ^2% = -48.5 ° ^(c = ^1, 95 95% A ^c ^ OH F: L. The c-Fmoc-SMS starting compound can be prepared as follows: 5g SMS acetate and 5g NaHCOe in 100 mL DMG / H2O 3: 1 was treated with 1.6 g Fmoc-HOS. After one hour at room temperature, the mixture was diluted with 400 ml of H 2 O and extracted with 250 ml of ethyl acetate / methanol 95: 5. The organic phase was dried with Na2SO4 and concentrated. Column chromatography on silica gel afforded the starting compound for the title compound as an amorphous substance; [o] 2 ° d = 24.3 ° (c = 1.13 DMF). Example XXXI. Using the procedure described in Example XXX, starting from okto-ac-tylccelebiozyloizot ^{arts and y} jan anu ^gave celebiozylotiotorbamjdo; N Formula ^70; [fr] ²⁰ D = - ^4.3 ° (c = ·! in AcOH), F: 0.87. 157 648 Example XXXII. By the method described in Example XXX, starting from 2,3,4,6-tetra-acetyl-): l-D-glucosylisocyanate, there was obtained (3-D-glucosylcarbamoyl-SMS of formula 71; [σ] ² d = -39.9 ° (c = 1 in 95% AcOH), F: 0.81. Example XXXIII. By the method described in Example XXX, celebiozylcarbamodoBNra of formula ^{72 was obtained starting from octa-acetylcelebiozylisocyamate;} [α] ² = ^{-37%, 9 C} (c = l in 95% AcOH), F: 0.85. . Example XXXIV. 1-Deoxy-D-sorbityl-SMS of the formula 73 0.5 mg of the title compound of Example 1 in 50 ml of methanol was treated first with NaBH4 and then with 5% acetic acid under such conditions that the pH did not rise above 7. The total consumption of NaBH4 was approximately 10 equivalents. After the reaction was complete (4-5 hours), the mixture was treated with acetic acid to destroy excess NaBFU. The mixture was concentrated in vacuo. The residue was demineralised e.g. with a duolite and purified on silica gel. The major compound besides 1-deoxy-D, mannithyl-SMS is the title compound which was obtained as a lyophilisate; [σ] d = -17.6 ° (c = 1 in 95% AcOH), F: 0.82. Example XXXV. By a method analogous to that described in Example XXXIV, starting from the title compound of Example II, aD-glucosyl (I44) deoxysorbityl-SMS of formula 74 was obtained; [σ] ² d = + 1.6 ° (c = 1 in AcOH), F: 0.9. Example XXVI. 1,2-dideoxy-srobityl-SMS of formula 75. 0.55 g of Boc-SMS in 30 ml of dioxane and water (3: 7) was treated with 50 mg of NaBHaCN. 250 mg of 2-deoxy-D-glucose was added. The pH of the mixture was adjusted to 7 with 0.1 ml HCl and heated to 100 ° C for 6 hours. The mixture was cooled, frozen and lyophilized. Ethyl acetate (50 ml) was added to the residue and shaken with water. The organic phase was dried and evaporated in vacuo. The Boc group was cleaved by conventional method with TFA. The product was purified on silica gel with demineralized, eg. Duolite to afford t ^y ° Tuł ^acid; [a] D ^{2 O} = ²⁵ 5 ° ^(c = 1% HOAc 95), FO, 83. The compound of Example XXXV (starting from maltose) can be prepared in an analogous manner. ^I n order ^k X ^XXVI I. -teoka ^ ^ ^ CHO esiMHAh ^{7 N-f} Uddeoks ruktoz ^ ^ o ^^ s ^11,18] kalcitonian salmon of formula 76, wherein R is a group of formula 77. ^{10.3 g of} N-isocaproHo-esiMKAia-catheitonin tosos-polyacetate ^{and 1.8 g of} D (+) -glucose were dissolved in a mixture of 94 ml of DMF and 6 ml of acetic acid. After 2 hours at 50 ° C, ether was added to completely precipitate the product which was suction filtered, washed with ether and dried in vacuo. For purification, the product (5-10 g) was dissolved in water, the solution was added to a 4 X 25 cm C18 reverse phase silica gel column and chromatographed with a gradient of water and 0-80% of a solvent mixture containing 38 parts of water, 60 parts of acetonitrile and 2 parts 85% phosphoric acid. The fractions that contained the crude product were combined, filtered through a column packed with about 100 mL of a weak base acetate ion exchange resin, and washed with water. The filtrate was lyophilized to give the title compound I ^{k p} of polyvinyl olih ^yd rat: [a] ^2% = - ^34.8 ° (c = ^{0.73, 95% CH 3 COOH),} F ^{1: 0.93,} FAB mass and ^pi spektrosko ³⁴⁰⁷ ( ^{MH +} ). Used as the starting compound peptide N ^σ Lysocaproyl-Ser-Thr-Als-Val-Leu-Gly-LysLeu-Ser-Gln-Glu-Leu-His-Lys-Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn -Thr-Asn-Thr-Gly-Scr-GlyThr-Pro-NH2 can be prepared as follows: a) N ^σ -isocaproyl-Ser (But) -Th - (But) -AiSlVal-Lru-OCH2-frnyl ° (p) OCH2-copolyri (polystyrene-1% -divinylbenzrn). 1 g of p-hydroxymethyl-froxymeryl-copolymer (polystyrene-1% -divinylbenzene) was allowed to swell in dimethylformamide in a mixture with methylene chloride 1: 4 (v / v), filtered through a vacuum filter and mixed with a solution of 0. 74 g of Fmoc-leucine and 0.19 g of 1-hydroxybenzotriazole in 5 ml of the abovementioned solvent mixture. While stirring, 0.43 g of dicyclohexylcarbodiimide and 85 g of 4-dimethylaminopyridine, each in 5 ml of the same mixture of solvents, were added. The mixture was stirred for 16 hours at 20 ° C, filtered through a vacuum filter and washed with a mixture of solvents followed by dimethylformamide. The obtained ί'm ° c-Lru-OCH2-phenyl- (p) -OCH2-copolymer (J polystyrene-1% -divinylbenzene). 157 648 The N ^ff -Fmoc group was cleaved from the resulting product (1.56g corresponds to 0.7 mol) by treatment with piperidine (20% v / v) in DMF for 10 minutes. Then washed thoroughly with DMF and 0.71 g Fmoc-Val-OH, 0.28 g 1-hydroxybenzotriazole and 0.32 g diisopropylcarbodiimide each dissolved in 5 ml DMF were added. After 45 minutes, the mixture was filtered through a vacuum filter and the peptide resin was washed thoroughly with DMF. The cleavage of the N®-Fmoc group was repeated and the linkage to the next amino acid in the sequence in the order given: Fmoc-Ala-OH (0.65 g) Fmoc-Thr (But) -OH (0.83 g) and Fmoc-Ser (But) -OH (0.80 g). In the last cycle, the reaction (cleavage of the Fmoc protecting group, acylating the protected amino acid (the amino acid derivative is replaced by izokapronowym acid (0.41 g), increased quantity. 1-hydroxybenzotriazole to 0.53 g of ^di- and zo crude ^{p l} for ^k ar ^{B i} m ^id u ^g to ^0.54, as rzęgania ^{p p} ditch ^{d and} t ^{o p} carnage ⁵ hours. WIC ^{Y E} of the peptide defended washed thoroughly with DMF and methylene chloride and dried under vacuum at 40 ° C for 15 hours and a resin with the protected peptide is obtained in the form of a colorless powder. b) Nff-isocaprooyl-Sei2 -Thr-Ala-Val-Leu-OH 1.0 g of N ^a -isocaproyl-Ser- (But) -Thr (But) -Ala-Val-Leu-OCH2-phenyl- (p) OCH2-copolymer (polystyrene-1% -divinylbenzene) was mixed in a mixture of 5 ml of acid trifluoroacetic acid and 5 ml of methylene chloride. The product was filtered off, washed with 5 ml of the same mixture and then with methylene chloride, concentrated significantly in vacuo and completely precipitated by adding ether. The precipitate was washed thoroughly with ether and dried in vacuo over solid potassium hydroxide to give the title compound as a colorless amorphous powder. c) ^{N ¢ f} -izoka ^{p ro} LO ^{S er-h} T R ^{A V} la- a] ^-Leu-G ly-L ^y s ^(B oc) ^-Leu-S er- ln ^{G, Gl} u ( ^OB u ') - Leu- ^H isLys (Boc) -Leu-Gln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2. To a solution of ^{0, 1, 65 g of} N ^0- -izoka ^p roilo- ^S er- ^T hr ^N Le ^{u-la- Val-OH in 7 ml DMF was added 0.59 g of} H-Gly-Lys (Boc - Leu -Ser-Gln-Glu (OBut - Leu-His-Lys (Boc - Leu-Gln-Thr-TyrPro-Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2, 0.017g 3 , 4-dihydro-3-hydroxy-4-oxo-1,2,3-benzotriazine, 0.065 g of dicyclohexylcarbodiimide and sufficient N-ethyl-N, N-diisopropylamine for a sample of the reaction mixture to show a pH of about 6 on wet pH indicator paper. The product was precipitated with ether for 16 hours and dried to yield the title product. d) Na-isocaproyl-Ser-Thr-Als-Val-Leu-Gly-Lys-Leu-Ser-Gln-Glu-Leu-His-Lys-Leu-GlnThr-Tyr-Pro-Arg-Thr-Asn-Thr- Gly-Ser-GIy-Thr-Pro-NH2. 0.50 g of the partially protected peptide from step c) was dissolved in a 50% v / v mixture. trifluoroacetic acid and methylene chloride. After 1 hour, 50 mL of ether containing 0.6 mol of HCl was added. The mixture was filtered, washed with ether and dried in vacuo. The product was purified by reverse phase chromatography with a gradient of acetonitrile in 2% N3PO4. The combined fractions containing pure material were filtered through a basic acetate ion exchange resin. The filtrate was lyophilized to give the title compound as polyvinyl pohhy ^d ratu; ^[A] ° D = - ^32.2 ° (c = ^0.3 in 9 ^5% Ac ^OH) R ^{0.87. Example} XXX ^V III. ^NFF - ^and zokapΓoiIo- (l- ⁴⁾ - ⁽⁷ and ^{Al, 18]} kalcytomna tososm of formula ^78, wherein R is a group of formula 79. The corresponding di-Nc-maltulosyl derivative was prepared by a method analogous to that described in Example XXXVII by using D (+) -maltose monohydrate instead of D (+) -glucose. The reaction time at 50 ° C was extended to 15 hours. Isolation and purification were the same to afford the title compound as a polyacetate, polyhydrate; FAB ^s pectates ^r ° ^s k ^op ia mass: ^3730, 9 (MH ⁺ X [a] D ^{2 O} = ^{- 15,} 2 ° ^(c = ⁰ 16, 95% AcOH) F: ^0, 97. Example XXXIX. Nf-isocaprooyl [Nf - (- deoxyfructosyl-Lys ⁷ ] salmon calcitonin (5-32) amide of formula 80; [ct] ²⁰ d = 4 ° C), 0 ° (c = 0, 27 in 95% AcOH), F: 0.84. ^{Example XL. S} posot> em-described ^{y p} y ^y m puts ^XXXV II to give N-Lys ¹ - ^ ^Ly s ^10N tris (l-deoksyfruktozylo) -kalcvtoninę salmon of formula 81, wherein R is a group of formula 82; [a]% = -5.3 ° (c = 0.38 in 95% AcOH), F: 0.75. ^P ΧΠ government ^kebab counters. ^Nff - ⁱ zo ^k a ^p roilo-des (l- ⁴ ) - [^ ίε- (l- ^d eo ^k s ^yf ructose ^{l o-- L} ys ⁷ ' ¹¹ ' ¹⁸ ] calc ^y salmon tonin (5-32) amide of formula 83, wherein R is a group of the formula 84 prepared in a manner described ^y m przykładlzie VH ^XXX, [α] = ^2% - ^37.4 ° (c = ^0.155, 95% AcO R ^ ^0.84. 157 648 25 Example XLII. Using the procedure described in Example XXI to afford N ^ff -chinoilo- [Ala ^7] łososia- calcitonin (5-32) -am ^id of formula 85; [σ] ² = ^ 35%, ⁷ ° (c = 0.37 95% AcOH), F: 0.88. ^P y ^yk order ^XLII I. ^S poso ^b I O ^p isan ^{y p} y ^y m chips ^χχι obtained ^Nf -chinoilo ^[A la ^7] kalc tonma ^y k> sosia- (4- ³²⁾ s ^d of formula ^86; [σ] ² = -39%, ³ R (c = ^{0.29 95%} AcOH ^ ^{F: 0,} 89. Wyjścrnwe ^p ept ^{-galactosides} [Ma ^ ^L -kalcytonma ososia- ⁽⁵ - ³²⁾ s ^{di [A} la ^7] -kalcytomna ^wit osos ^and a- ⁽⁴ - ^{32) required} in examples XLII and XLIII may be prepared by a method analogous to that described in example XXXVII the preparation of starting material. ^{Example XL} IV. ^[N -deo ^k s ^y -fruktoz ^yl oC ^y s ^1] -oksytocyna of formula ^87. 0.5 g of D (+) -glucose and 0.5 g of oxytocin were dissolved in 50 ml of MeOH / HOAc 9/1 and kept at 65 ° C for 3 hours. The solution was then concentrated by evaporation, chromatographed on silica gel and freed from the salt by Duolite (HaO) - (ethanol / HOAc gradient). A white lyophilisate was obtained; [ct] ²⁰ d = -23 ° (c = 0.32 in 95% HOAc), F: 0.95. Example XLV. 60 mg Ac- (D) Phe (4Cl) - (D) Phe (4-Cl) - D) Trp-Ser-Tyr-D (D> -Lys-Leu-ArgPro- (D) Ala-NH2 and 72 mg of D (+) glucose was dissolved in a mixture of 10 ml of MeOH and 1 ml of AcOH and stirred at 60 ° C for about 20 hours. The product was precipitated with ether and filtered. The residue was dissolved in about 100 mg of H 2 O and the pH was adjusted to 8 with dilute NaOH. The product was adsorbed on a column of Duolite ES861 and eluted with a gradient of HAO-dioxan-FkOAcOH (60: 40: 3). the fractions containing the desired product were concentrated in vacuo then subjected Hofilizacji. ^the inside ^y mano zwózek of formula ^88; [α] ^2% = - ²⁵ ° C (c = ^0.5 in ⁹ 5% AcOH), ^{F: 0.83.} Y ^{P y} I. ^N EXAMPLE ^{XLV <FA1, NffB1, Nf B29} -tris (l-deoks fruklozy ^{y l} o} ^{-porcyno-insu)} ina. A suspension of 1 g (0.17 mmol) of porcine-insulin and 0.47 g (2.6 mmol) of glucose in 10 ml of a 9: 1 mixture of dimethylformamide and acetic acid was stirred at 60 ° C for 1 hour. The solvent was removed at 30 ° C under high vacuum. The residue was dissolved in 300 ml of H 2 O, the pH was adjusted to 7 and the mixture was passed through a small demineralization column (Doulite ES 861 2.5 × 15 cm). The glucose was washed with water and the peptide was washed with isopropanol / water / ethyl acetate 59: 39: 2. The solvent was removed and the mixture was freeze-dried. 300 ml of water was added to the residue and purified by reverse phase chromatography. (2X25 cm column, RP 18, 10 nm, buffer 57 mmoles NaCICL, 20 mmoles triethylamine, 8.4 mmoles phosphoric acid, pH 3 with 4N NaOH, gradient 0-65% AB. Buffer A buffer pH 3 / ac ^^ onitryI 9: 1; Buffer B buffer pH 3 / acetonitrile 4: 6. Fractions containing the title compound were collected, combined, concentrated, diluted with 300 mL of water and passed through the demineralization column described above. The salts were washed off with water. The peptide was eluted with isopropanol / water / ethyl acetate 59: 39: 2. Appropriate fractions were combined ^and congested ^{concentrations} intra- it will wipe ^{y k} zw ^ble with the title; [α] ² % = ^56.3ο, (c ^{= 0.5 A} c ^OH ), ^F : ^0.88 . Example XLVII. Using an analogous procedure to that described in Example XXXVII, coming out of ^a section of [la ^{DA 2] H} p F ^GR will wipe ^y mano ^Ν σ, ^Ly s ¹² - ^{£ N, Ly} s ²¹ - ^Nί tris ⁽⁾ - roks ^{d) y} ruktozylo) - / ^{D [a} la ^{2] HPG R} F (2 ^ ^{9) -} ^^ FU of formula ^89, wherein ^Y m ^R ru ^{g PE} of formula ^90; [σ] ^Μ ο - -5.6 °, (c = ^0.2 in 95% AcOH), F: 0.82. ^P y ^yk order ^XLV HI. ^{NFF, NC-b and} s (l-deoks fruklozy ^{y l} o) Lys-vasopressin of formula 91, wherein R is a group of formula 92. ^ wtesmę Π8 mg ^(0.1 mmob) ys ^{L y y} -vasopressin ³⁶⁰ mg ⁽² mmok) ^gl ukozy in ⁵ m ^l of methanol / ethyl acetate 9: 1 was stirred at 65 ° C for 2 to 4 hours. The solvent was removed in vacuo. 30 ml of water was added to the residue and the solution was lyophilized. To remove excess glucose, the peptide (solution in 40 ml of water, pH 7.3) was adsorbed onto a Duolite column (1.5 X 10 cm). Glucose was eluted with water and the peptide was eluted with isopropanol / water / ethyl acetate 59: 39: 2. The mixture was purified on a silica gel column (eluent: chloroform / methanol / ethyl acetate / water 7: 4: 1: 1). Fractions containing the title compound were concentrated and lyophilized to afford the title compound; [cr] 20 _{D =} -52 ", (c = 0.5 in 95% HOAc), F: 0.84. Example XLIX. Formula 93 was prepared as described in Example XLV starting from Ac- (D) Phe (pCl - (D) Phe (pCl - (D) -Trp-Ser-Lys- (D) Phe-Leu-AΓg-Pro. - (D-AlaNH2, acetate and (D (+) -glucose; [a] □ = -36 ° (c = 0.5 in 95% AcOH), F: 0.86. Example L. Compound of Formula 94 was prepared analogously to Example XLV starting from H- (D) Phr (pCl> - (D) Phr (pCl) - (D - TΓp-Ser-Tyr- (D) -Phr -Lru-ArgPr ^o - (D) -NH ^{2 and} Al ^as cta ^{n g} u TOK ^eskers D ^(+); [ff] ²⁰ D = -32 ° (c = ⁰ 5 in 95% AcOH) F: 0.94. 157 648 Example LI. 200mg H- (D) Phe (pCl) - (D) Phe (pG1HD) Trp-Ser-Tyr- (D) Lys-Leu-Arg-Pro (D) Ala-NH ² i 5 ² 0 m ^g D (+ ) ^{g y} lukoz in DMF / AcOH 15: 1 was stirred at 60 ° C for 3 ^g odzir ^y. The mixture was concentrated in vacuo, precipitated with ether, filtered and dried. The residue was purified as follows: 1) Adsorption on Duolite ES 861 and elution with dioxane-HzO-AcOH mixture, 2) Silica gel column chromatography using as eluent CHCl3 (AcOH) H ₂ O, 3) Preparative liquid pressure chromatography ("reverse phase") on an octadecyl silica gel column. Elution with an acetonitrile gradient in 2% H3PO4. The fractions that contained the leading compound were combined, filtered through a column of weak basic acetate ion exchange resin, concentrated and lyophilized to afford the title compound; [ar] 2 ° d = 22.6 ° (c = 0.5 in 95% AcOH), F: 0.63. 157 648 R-iDJF ^ ł ^ c ^ ipCC-K ^ Jfpheifp ^ lJ-tDITrp-Ser- ^ Tyr R - (D) Lys -Leu-Arg - Pro- (D) Ala- NH2 PATTERN 95 A ^c - (D) Phe (pCl) - (D) Phe ( ^p Cl) - (D) Trp-Ser- Lys ( ^N * - (D) Phe-Leu-Arg-Pro- (D) ALa-NH2 CH3COOH H PATTERN 93 H ⁽ - ⁹ OH 1 \ H HO / I Ηθ \ __ / HD) Phe ( ^p C l) - (D) Phe ( ^p C l) - (D) Tr ^p - Ser - Tyr - (D) Phe OH H -Leu-Arg-Pro-fDIAla-N ^ CHgCOOH MODEL 94 R AND R- Cys-Tyr-Phe-Gln-Asn-Cys-Pro-Lys-Gly-NHo I --- I PATTERN 91 R 1 2 * 12 R-Tyr-D-Ala-Asp-Ala-lle-Phe-Thr-Asn-Shr-Tyr-Arg-Lys-Val-Lhu-Gly29 Gln-Leu-Ser-Ala-Arg-Lys-teu-Lhu-Gln-Asp-lle-Met-Shr-Arg-N ^ CH ^ COOH R MODEL 89 (D) Lys {N ^Z '-CH 2 HO <OH ^ OH-) - Lhu-Arg-Pro- (D) Ala-NH2 OH MODEL 88 OH H. CI - ^ - Cys-Tyr-Ilh-GLn-Asn-Cys-Pro-Lhu-Gly-N ^ A GOOD DEATH: 87 157 648 5 7 CX) -Ser-Thr-Ala-Val-Leu-Gly-Lys-Leu-Ser-Gln-GLu-Leu-H is-Lys Leu-Oln-Thr-Tyr-Pro-Arg-Thr-Asn-Thr-iGy -SSr-Gly-Thr-Pro-NI- ^ · 3CH.0OOH FORMULA 85 4 7 OLu-Ser-Thr-ALa-Vai-Leu-Gty-Lys-Leu-Ser-Gln-GLi-Lru-His32 Lys-Lru-Gin-Thr-TTr-Pro-Arg-Thr-Wsn-Thr-Gtyr-Sr-Gly-Thr-Pro-NH ,? 3CH-C00H MODEL 86 with i CH3CH3 CH ch _l 7 n I and ₇ in CH2-CO-Ser’Thr-Lys-Val-Leu-Gly-LLy-Ljeu-Ser-G-n - Glu-ljru-HisR Hl 32 -Lys-Jrw-Gln ^ Thr-TTr-FPo-Arg-Thr-Asn-Thr-GlyrSer-Gly-Thr-Pro-N ^, -, io R - Cys - Ser- Asn - Leu - Se- -Th- - Cys-Val- Leu -Gy-Lys-Leu - Se - -Gln-Gu -Leu-His-Lys-Leu-Gln-Thr-TTi ^ Pro -Arg-Thr-Asn-Thr-Gly-Ser-Gly-Thr-Pro-NH2 PATTERN 81 157 648 PATTERN 82 CH? - CO - Ser-Thr- Lys-Val-L £ u-Gly-Lys-L ^ -ae- (Gn - Glu-b2u-His-L) S-Leu32 -Gln-Thr-TyrrPro-Arg-Bir-Asn-Thr-Gly-Ser-Gty-Thr-PiO-M ² · 3 C ^H ^ C ^OOH PATTERN 80 Ho CHo ^J ^ CH ^ ³ I. C Ho R And ⁷ fu and e CH ^ - CO-Ser-Thr -Ala-Val-Leu-Gly-Lrs -Leu -Ser-Gln-Glu-Leu -His-LysI R -L £ uGln-Thr-Trr-ProAArg-Thr-S £ T-Thr- (y - Sr - Gly - Thr-Ffo-NH2CHjCOOH MODEL 78 PATTERN 77 157 648 OH OH (D) Phe - Cys-Phe - (D) Trp- Ly ^^ Thr- Cys-Thr- ol PATTERN 75 ch ₂ R hi CH? - CO - Ser -Tir-Ala -Val -Leu - ^ 1 ^ -Lys -Leu -Ser -Gin -Glu -Leu - H is -Lys ^z I R Leu-Gln-Thr-Tyr-Pro -Arg-7hr-A \ sr-TTh - Gly-Ser-Gly-Thr- Pro-NH? CH? CCCH MODEL 76 (D) ^ph e C ^{y s-ph} e ^{- (D) y} L ^T rp s-Thr-Cys-Thr-ol. CH CH CH CH MODEL 73 PATTERN 71 PATTERN 67 157 648 HoC -Ć - C- (DPhe -Cys-Phe- (D) Trp-Lys-Thr-Cys-Thr-ol ° (R) i '> MODEL 68 H0Hi CH ₃ 0 --H I -3 u H, —0 0 _- y - 0- C - C- (D) Phe - Cys-Phe-D) Trp - Ly - hr-Cyy-Thr-ol HO H OH CH3 PATTERN 66 HO H. -H \ 0H Η / HOy—— | H H OH • och ^ (DTPhe -Cys-Phe- {D) Trp-Lys-Thr-Cys-Thr-ol PATTERN 64 157 648 PATTERN 59, -, C - (D) Phe-Cys-Phe - (D) Trp-Lys-Thr-Cys-Thr-oL H OH PATTERN 60 HO HO -O \ χ- / χ-0Η, -, (D) Phe —Cys-Phe- (D) lrp-Lys-Thr-Cys-Thr-ol PATTERN 57 157 648 HO HO- OH .OH (D, Phe-Ćys-Phe- (D) Trp-Lys-Thr- Cys-Thr -ol PATTERN 58 <CH ₂ - (D) Phe-Cys-Phe- (D) Trp-Lys-Thr-Cys-Thr-ol OH OH PATTERN 55 R- (D) Phe-Cys-Phe - (D) Trp-Lys -Thr- Cy ^^ TIrr ^ ol MODEL 52 About II HO-P-OCH2 OH I 1/0 ' OH (D) Phe -Cys-Phe - (D) Trp-Lys-Thr-Cys-Thr-ol MODEL 54 MODEL 49 ^1- e- ¹ R - (D) Phe-Cys-Phe- (D) Trp-Lys-Thr-Cys-Thr-ol FORMULA 50 H. HJ— °> OH \ H HO / i-> HO ψ — f CH ₂ - (D) Phe-Cys-Tyr- (D) Trp-Lys-Thr-Cys-Thr-ol HO H PATTERN 47 PATTERN 48 MODEL 46 MODEL 42 MODEL 43 H. H ' OH OH2-SMS MODEL 44 157 648 Η HO OH, OH ĆH2 - (D) Plh-Cys-Phe- (D) Trp-Lys-Thr-Cys-Thr-ol CH3COOH PATTERN 37 - Oh, MODEL 38 OH CH2-NH-Q ' Ge / ^ oo-ę'MODE 35 MODEL 34 PATTERN 36 OH PATTERN 33 PATTERN 31 ... About QH% x Lf CH2WZOR 32 Z A CH-S-Y Y-S-CH. I I I 2 1 1 | 2 -CH-CO-N-CH-CO-B-C-D-E -NH-CH-F PATTERN 30 S. CO-N— | —Χί PATTERN 29 MODEL 28 MODEL 27 CH, CO-CH FORMULA 25 < ^CH 2> n - O / ^ n = c = l PATTERN 23 CO-NH-CH-COOR I ^{e R} d PATTERN 26 -CO-C- (CH ₂ ) _m -H ^R b PATTERN 24 θ4> ^ NH-Q-NH-LHRH-Antag PATTERN 19. '• O G /; ^ vO-Q’-NH-LHRH-Antag MODEL 20 HOCt ^ C - (CHOH) _c - C-CH ₂ -NH-LHRH-Antag Y PATTERN 21 NH - CO - CH ₂ - CH ₂ - CO PATTERN 22 G ₃ -CO-NH-LHRH-Antag MODEL 18 ^R f ^A f ^B fCf f ^E i ^F i ' ^G f ^H PATTERN 16 - lo - Ko -NH2 NH-LHRH-Antag FORMULA 17 y; AND* Ch ^ - SH R - (NH- CH-CO) - Αθ-NH-CH -CO-Αθ Ag-: PATTERN 12 ch ₂ -sr ₁₀ R _n -V - CH - CO ^ 1 ₂ MODEL 13 Yj C ^h 2 ^{- sr} 10 R- (NH-CH -CO) _o -A ₆ -NH-CH-CO-A ₈ FORMULA A and G-CO-N-Calc CH0-SH I ² R _n -V-CH-COR ₃ FORMULA 15 ^ -ProN ^> g-Zi-ProNH2 PATTERN 11 c 157 648, - 0 4α T ^ NH-Q-ΝΗ-CaLc (Q = CO or CS) PATTERN 11 c HOł ^ C - (CHOH) c - CY-CHjNH - Inches θ2 V <zx ^ OH 'NH-Calc ^Ó 4 λ ( 0-Q '-N - Inches PATTERN 11 b PATTERN 11 d R ₅ I ⁵ -CH-X] PATTERN 9 ^Y and ^Y 2 ¹ and ^Lc R- (NH- OH- CO) _o - Ag-NH-CH-CO-Ag-Ag-Zj-ProN ^ PATTERN 10 ... About θ ^Η CH ₂ - NH - Inches MODEL 11 a Δ 'CH, -SY, y ₂ -s-ch ₂ HOCH ₂ - (CH ^ H) c-CY-CH2-N-iCH-ON-CH-CO-BCDE-NH-CH-F PATTERN 8t Z, ∆ CH ^ -S-Y. Y, -S-CH, I ¹ II 2 I 2 IZ A ^P -NH-CH-CO-N- CH 1 2 CO-B-C-D-E-NH-CH-F 3 4 5 4 »7 PATTERN 8 pa AZ Δ CHl-S-Υ. Y <S-CHo II II ^{2 1 2} I ² G-CO-N-CH-CO-N-CH-CO-B-C-D-E-NH-CH-F 1 2 3 4 5 6 7 PATTERN 8 bp AZ A 'CFk-SY. Y <s-CHII II ^{2 1 2} I ² O-O-C- K-cCO-N-HH-CO-N - CH-CO-B-C-D-E-NH-CH-F 1 2 3 4 5 6 7 MODEL 8 pc fl f ^ęH 2-s-Yi Y ² -s-ch ₂ OH-CO-N-CH-CO-B-C-D-E-NH-Ch-F MODEL 8e A 'CH <S-Yi i I 2 1 Υ, - S-CH. 2 and 2 A-NH- CH - CO-N-CH-CO- B - C-D-E -NH-CH-F 1 2 3 4 5 6 7 MODEL 8 Ω 0H Z. A CH, -S-Y, Y < S-CH. I ¹ II ² 1 2 | 2 CH2- nh-ch-co-n-ch-co-b-c-d-e -nh-ch-f FORMULA 8a, ~ O? 2 S ^ OH Ί ,, i i A 'CH2-S-Y, Y2-S-CH2 NH-CH-CO-N-CH-CO- B-C-D-E-NH-CH-F PATTERN 8b. A 'CHyS-Y. ¹ II ^{2 1} y ₂ - sc h ₂ G ₃ -CO-N-CH-CO-N-CH-CO-BCDE-NH-CH-F PATTERN 8c .-. O A CH ^ S-Y] Y2-S-CH2 G4 ^ X ^ oO-Q ' ^-N -CH ^- CO-N-CH-CO-BCDE-NH-CH-F PATTERN 8d HOH ₂ C - tCHOH) _c - CY - CH ₂ - NH -P FORMULA 5 a HOH ^ C - (CHOH) c- CY - CH2 FORMULA 5 a ' HOHC- (CHOH) - CH - CH OH 2 c | 2 NHP PATTERN 5b HOH-C- (CHOH) - CH - CH-OH 2 c 1 2 PATTERN 5b ' MODEL 7b MODEL 6a CH2-NH -Q NH-Q PATTERN 4c ' PATTERN 4 a 'o-' PATTERN 4 b ' NH -Q "MODEL 4d" ...- 0 G4 ^^ nh-q-n -p PATTERN Aa R _y , -0. » ^Y GA Ys / O) -Q'-N-P , ... O O Ry / ^ CH - NH -O ’“ N - P PATTERN Ac PATTERN Ab NH-Q "'- N-P WZOR Ad X -NH-P PATTERN 1 PATTERN 1 ' PATTERN la PATTERN 2 a G ₃ -CO-NRy-P PATTERN 3