IDENTIFICATION OF THE GLYCOSYLATED SEQUONS OF HUMAN MYELIN-ASSOCIATED GLYCOPROTEIN

被引：17

作者：

BURGER, D ^{[1
]}

PIDOUX, L ^{[1
]}

STECK, AJ ^{[1
]}

机构：

[1] CHU VAUDOIS, DEPT NEUROL, NEUROBIOL LAB, LAUSANNE, SWITZERLAND

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1993年 / 197卷 / 02期

关键词：

D O I：

10.1006/bbrc.1993.2501

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：

Myelin-associated glycoprotein (MAG) is a neural cell adhesion molecule expressing the L2/HNK-1 carbohydrate epitope. MAG is heavily glycosylated containing 30% carbohydrate by weight. In this study, human MAG glycopeptides were isolated and sequenced. Of the 9 MAG sequons 7 were glycosylated and 1 was partially glycosylated at Asn106. Asn332 which was not recovered in the glycopeptide fractions was probably not glycosylated. Furthermore, preliminary data indicate that all MAG glycosylated sequons might bear the L2/HNK-1 epitope. © 1993 Academic Press, Inc.

引用

页码：457 / 464

页数：8

共 23 条

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