Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid‐containing Ser/Thr‐linked carbohydrate chains of N‐terminal octapeptides from human glycophorin A

FEBS Letters

Yamamoto, Kazuo¹  Osawa, Toshiaki¹  Irimura, Taturo¹  Konami, Yukiko¹ 

[1] Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, The University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: Maackia amurensis hemagglutinin;    Lectin affinity chromatography;    Carbohydrate-binding specificity;    Human glycophorin A;    Sialic acid-containing Ser/Thr-linked carbohydrate chain;    Fetuin-GP-Sepharose;    fetuin-glyeopeptides-Sepharose 4B;    MAH;    Maackia amurensis hemagglutinin;    MAL;    Maackia amurensis leukoagglutinin;    PSM;    porcine submaxillary mucin;   

DOI  :  10.1016/0014-5793(94)80527-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 Neu5Acα→3Galβ1→3(Neu5Acα2→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.

【 授权许可】

Unknown