Title : Studies on the binding substances on human erythrocytes for the heat-labile enterotoxin isolated from porcine enterotoxigenic Escherichia coli.

Pub. Date : 1989 Apr 14

PMID : 2649154






3 Functional Relationships(s)
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1 The binding of 125I-labeled LTp to neuraminidase-treated human type A erythrocytes was most effectively inhibited by ganglioside GM1 among inhibitors used. G(M1) Ganglioside neuraminidase 1 Homo sapiens
2 On the other hand, hemagglutination of neuraminidase-treated human type A erythrocytes by LTp was inhibited by methyl alpha-D-galactopyranoside, galactose, melibiose and some glycoproteins, but not effectively inhibited by ganglioside GM1 at the highest concentration used. G(M1) Ganglioside neuraminidase 1 Homo sapiens
3 Although these findings show that there may be fundamental differences between interactions with ganglioside GM1 in hemagglutination compared to interactions with ganglioside GM1 in binding, the predominant binding substance for LTp on neuraminidase-treated human type A erythrocytes is suggested to be ganglioside GM1. G(M1) Ganglioside neuraminidase 1 Homo sapiens