title: Strong affinity of Maackia amurensis hemagglutinin (MAH) for sialic acid-containing Ser/Thr-linked carbohydrate chains of N-terminal octapeptides from human glycophorin A.
abstract: 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.
authors.affiliation: Division of Chemical Toxicology and Immunochemistry, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
authors.forename: Y
authors.initials: Y
authors.lastname: Konami
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: T
authors.initials: T
authors.lastname: Osawa
authors.forename: T
authors.initials: T
authors.lastname: Irimura
mesh_terms: D002240:Carbohydrate Sequence; D002846:Chromatography, Affinity; D006021:Glycophorins / Q000737:chemistry*; D006801:Humans; D066298:In Vitro Techniques; D008969:Molecular Sequence Data; D010835:Phytohemagglutinins / Q000378:metabolism*; D037121:Plant Lectins; D012639:Seeds / Q000737:chemistry; D012795:Sialoglycoproteins / Q000378:metabolism*; D013329:Structure-Activity Relationship
chemical_list: D006021:Glycophorins; D010835:Phytohemagglutinins; D037121:Plant Lectins; D012795:Sialoglycoproteins