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Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid‐containing Ser/Thr‐linked carbohydrate chains of N‐terminal octapeptides from human glycophorin A
Author(s) -
Konami Yukiko,
Yamamoto Kazuo,
Osawa Toshiaki,
Irimura Taturo
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80527-x
Subject(s) - glycophorin , tetrasaccharide , chemistry , biochemistry , lectin , hemagglutination , sialic acid , hemagglutinin (influenza) , affinity chromatography , glycopeptide , carbohydrate , sialoglycoproteins , stereochemistry , membrane , biology , antigen , polysaccharide , enzyme , antibiotics , gene , genetics
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.