STRONG AFFINITY OF MAACKIA-AMURENSIS HEMAGGLUTININ (MAH) FOR SIALIC ACID-CONTAINING SER/THR-LINKED CARBOHYDRATE CHAINS OF N-TERMINAL OCTAPEPTIDES FROM HUMAN GLYCOPHORIN-A

被引：76

作者：

KONAMI, Y ^{[1
]}

YAMAMOTO, K ^{[1
]}

OSAWA, T ^{[1
]}

IRIMURA, T ^{[1
]}

机构：

[1] UNIV TOKYO,FAC PHARMACEUT SCI,DIV CHEM TOXICOL & IMMUNOCHEM,BUNKYO KU,TOKYO 113,JAPAN

来源：

FEBS LETTERS | 1994年 / 342卷 / 03期

关键词：

MAACKIA AMURENSIS HEMAGGLUTININ; LECTIN AFFINITY CHROMATOGRAPHY; CARBOHYDRATE-BINDING SPECIFICITY; HUMAN GLYCOPHORIN A; SIALIC ACID-CONTAINING SER/THR-LINKED CARBOHYDRATE CHAIN;

D O I：

10.1016/0014-5793(94)80527-X

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：

The interaction of the Maackia amurensis hemagglutinin (MAH) with various glycopeptides and oligosaccharides was investigated by means of immobilized lectin affinity chromatography. An amino terminal octapeptide obtained from human glycophorin A having three Neu5Ac alpha 2-->3Gal beta 1-->3(Neu5Ac alpha 2-->6)GalNAc tetrasaccharide chains, designated as CB-II, was found to have an extremely strong affinity for MAH. Therefore, it is strongly suggested that hemagglutination by MAH was caused by its interaction with Ser/Thr-linked carbohydrate chains of human glycophorin A on erythrocyte membranes.

引用

页码：334 / 338

页数：5

共 27 条

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