Synthesis and properties of some serine glycosides

Derevitskaya, V. A.; Vafina, M.G.; Kochetkov, Nikolay K.

doi:10.1016/s0008-6215(00)82214-4

Cited by 67 publications

(9 citation statements)

References 10 publications

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“…higher than 10000. In view of the composition of this fraction (Table 1), it appears unlikely that all the threonine residues involved in glycosidic linkages were in a terminal position and therefore resistant to cleavage (Derevitskaya et al, 1967). Kieras (1974) also found alow conversion ofdestroyed threonine into r-aminobutyric acid in keratan sulphate glycopeptides, but the data presented suggested that this was caused by incomplete reduction of the unsaturated product formed by the fl-elimination reaction.…”

Section: Discussionmentioning

confidence: 95%

The isolation and partial characterization of the major glycoprotein (LGP-I) from the articular lubricating fraction from bovine synovial fluid

Swann¹,

Sotman²,

Dixon³

et al. 1977

Biochemical Journal

113

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The articular lubricating fraction from bovine synovial fluid was prepared by repeated fractionation in three consecutive CsCl density gradients to remove completely traces of hyaluronic acid. The major glycoprotein consituent (LGP-I) was then isolated by repeated gel-permeation chromatography. The yield of the LGP-I component was about 20 mg/litre of synovial fluid. Sedimentation-equilibrium measurements showed that this glycoprotein was homogeneous and the mol.wt. was calculated to be 227500. Amino acids represented 43% (w/w) and carbohydrate constituents 44% (w/w) of the molecule. Threonine, glutamic acid, proline and lysine (224, 127, 242 and 128 residues/1000 residues respectively) were the major amino acids. Galactosamine, galactose and N-acetylneuraminic acid (202, 162 and 114 residues/molecule of LGP-I component respectively) accounted for 98% of the total carbohydrate residues present. Small amounts of mannose and glucosamine (1 and 9mol respectively/mol of LGP-I component) were also present. After treatment of LGP-I component with alkali and NaB3H4 radioactivity was incorporated into alpha-aminobutyric acid and alanine in a molar ratio of 4:1, and radioactive galactosaminitol was isolated by ion-exchange chromatography from a cleaved oligosaccharide fraction. These data demonstrate the presence of threonine and serine -O-GalNAc linkages, but only 25% of the theoretical likages involving threonine were cleaved by a beta-elimination reaction. Digestion of LGP-I component with Pronase followed by chromatography on DEAE-cellulose yielded glycopeptide fractions with a similar amino acid and carbohydrate composition to the intact molecule. Treatment of desialylated and intact LGP-I component with galactose oxidase followed by reduction with NaB3H4 revealed the presence of 52mol of terminal galactose in the intact molecule and 153mol of galactose/mol of LGP-I component after treatment with neuraminidase. The data indicate the LGP-I component is composed of a single polypeptide chain containg more than 150 oligaosaccharide side chains composed of O-GaINAc-Gal distributed over the length of the peptide chain and that terminal sialic acid residues are linked to galactose in two-thirds of these side chains.

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Section: Discussionmentioning

confidence: 95%

The isolation and partial characterization of the major glycoprotein (LGP-I) from the articular lubricating fraction from bovine synovial fluid

Swann¹,

Sotman²,

Dixon³

et al. 1977

Biochemical Journal

113

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“…The changes in the major amino acids and the amino sugars are summarized in Tables 2 and 3. It has been shown that both the amino and carboxyl groups of O-glycosidicallylinked hydroxy amino acids must be substituted in order for /3-elimination to occur (RILEY, TURNBULL and WILSON, 1957;PHOTAKI, 1963 ;DEREVITSKAYA, VATINA and KOCHETKOV, 1967). Rat and rabbit brain glycopeptides treated with 0.4 M borohydride in 0.02 N NaOH for 16 h at 45°C (Conditions B) gave the highest recoveries of alanine (80-106 per cent) and a-aminobutyric acid (56-65 per cent) relative to the amounts of serine and threonine destroyed.…”

Section: R E S U L T Smentioning

confidence: 99%

Carbohydrate‐peptide Linkages in Glycoproteins and Mucopolysaccharides From Brain

Atherton

1972

Journal of Neurochemistry

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Abstract— Treatment of glycopeptides, prepared from glycoproteins of rat and rabbit brain, with NaOH‐NaBH4 leads to the destruction of a portion of the serine, threonine and galactosamine present, and the appearance in acid hydrolysates of alanine, α‐aminobutyric acid and galactosaminitol. These results indicate that N‐acetylgalactosamine at the reducing end of oligosaccharide chains in brain glycoproteins is linked O‐glycosidically to the hydroxyl groups of serine and threonine residues. 2‐acetamido‐1‐(L‐β‐aspartamido)‐l,2‐dideoxy‐β‐D‐glucose was also detected after partial acid hydrolysis of the alkali‐stable glycopeptides, and most of the carbohydrate in brain glycoproteins appears to be linked by N‐acetylglucosaminylasparagine linkages. The results of the treatment of the sulphated mucopolysaccharides from bovine brain with alkaline‐borohydride indicate that the polysaccharide chains in chondroitin sulphate and heparan sulphate are linked exclusively to serine.

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“…The presence of xylose and galactose together with 4-sulphated chondroitin chains bound to membrane fractions argues for the close relationship of these saccharides with the serine-linked macrostructure that comprises most of the extracellular matrix. The possibility remains that the alkali-stable fraction still contains saccharide chains attached to peptide via the fl-xylosyl-serine linkage, but that the serine residue is at the terminus of a polypeptide chain and thus does not readily undergo the characteristic #-elimination reaction (Derevitskaya et al, 1967).…”

Section: Fig 2 Chromatography Of Polysaccharide Frommentioning

confidence: 99%

“…But not all O-glycosidic linkages Vol. 126 involving serine residues in which both the oc-amino and a-carboxyl groups are blocked are readily split by alkali (Derevitskaya et al, 1967). A second possibility is that the polypeptide core is still intimately associated with the membrane structure such that its interaction with alkali does not result in the characteristic ,-elimination reaction.…”

Section: Fig 2 Chromatography Of Polysaccharide Frommentioning

confidence: 99%

Protein–polysaccharide biosynthesis. Membrane-bound saccharides

Derge

Davidson

1972

Biochemical Journal

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Membrane-bound saccharides obtained from ear cartilage from rabbits recovering from papain injection were examined for glycosyl acceptor properties, alkali lability, molecular size and degree of sulphation. Although considerable glucuronosyl transfer from UDP-glucuronic acid could be demonstrated, less than one-third could be identified as representing chondroitin linkage formation; there was little or no effect of molecular size on acceptor properties. Approximately one-half of the membrane-associated chondroitin-like saccharide chains are solubilized by alkali, whereas one-half require proteolysis for solubilization. These fractions are analytically indistinguishable and both contain xylose and galactose as well as uronic acid and sulphated N-acetyl-galactosamine. All fragments that were examined contained stoicheiometric amounts of axial sulphate ester, strongly suggesting a close relationship between chain extension and sulphation.

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Synthesis and properties of some serine glycosides

Cited by 67 publications

References 10 publications

The isolation and partial characterization of the major glycoprotein (LGP-I) from the articular lubricating fraction from bovine synovial fluid

The isolation and partial characterization of the major glycoprotein (LGP-I) from the articular lubricating fraction from bovine synovial fluid

Carbohydrate‐peptide Linkages in Glycoproteins and Mucopolysaccharides From Brain

Protein–polysaccharide biosynthesis. Membrane-bound saccharides

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