CHARACTERIZATION OF A GLYCOPEPTIDE FROM PATHOLOGICAL HUMAN-IGM WITH AN UNUSUAL OLIGOSACCHARIDE CORE

被引：4

作者：

JOUANNEAU, J

BOURRILLON, R

机构：

[1] Laboratoire de Biochimie (U. 180 INSERM), Faculté de Médecine, 75006 Paris, 45, rue des Saints-Pères

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1979年 / 91卷 / 03期

关键词：

D O I：

10.1016/0006-291X(79)91987-9

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：

A glycopeptide from human pathological IgM has been prepared and characterized. It contains an unusual oligosaccharide core with only one N-acetylglucosamine carrying six mannosyl residues, and linked to the asparagine. The involvement of sugar has been determined by use of α and β mannosidases and endoglycosidase digestions. The amino acid sequence has been elucidated and from the obtained data it could be located on the C terminal portion of the IgM Du heavy chain at the Asn 563. This glycopeptide is characterized by the absence of a N-N-diacetylchitobiose unit in the oligosaccharide moiety and its condensed structure is proposed: {A figure is presented}. © 1979.

引用

页码：1057 / 1061

页数：5

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