BOVINE COLOSTRUM CMP-NEUAC-GAL-BETA(1-]4)GLCNAC-R ALPHA(2-]6)-SIALYLTRANSFERASE IS INVOLVED IN THE SYNTHESIS OF THE TERMINAL NEUAC-ALPHA(2-]6)GALNAC-BETA(1-]4)GLCNAC SEQUENCE OCCURRING ON N-LINKED GLYCANS OF BOVINE-MILK GLYCOPROTEINS

被引：28

作者：

NEMANSKY, M

VANDENEIJNDEN, DH

机构：

[1] Department of Medical Chemistry, Vrije Universiteit, 1081 BT Amsterdam

来源：

BIOCHEMICAL JOURNAL | 1992年 / 287卷

关键词：

D O I：

10.1042/bj2870311

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Bovine colostrum CMP-NeuAc:Galbeta(1-->4)GlcNAc-R alpha(2-->6)-sialyltransferase (alpha6-sialyltransferase) appears to be capable of catalysing alpha6-sialylation of the disaccharide GalNAcbeta(1-->4)GlcNAc to yield the trisaccharide NeuAcalpha(2-->6)GalNAcbeta(1-->4)GlcNAc. This provides an enzymic basis for the occurrence of this sialylated structure on the N-linked glycans of a number of bovine milk glycoproteins. Competition experiments using Galbeta(1-->4)GlcNAc and GalNAcbeta(1-->4)GlcNAc as acceptors indicate that both substrates are recognized by a single active site on the alpha6-sialyltransferase. Extrapolation of these results suggests that the NeuAcalpha(2-->6)GalNAcbeta(1-->4)GlcNAc structural element occurring on the N-linked glycans of several human glycoproteins are similarly synthesized by the action of a Galbeta(1-->4)GlcNAc-R alpha(2-->6)-sialyltransferase.

引用

页码：311 / 316

页数：6

共 31 条

[1]

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