Studies of the ligand binding to cholera toxin, II. The hydrophilic moiety of sialoglycolipids.
Hoppe Seylers Z Physiol Chem
; 358(2): 159-63, 1977 Feb.
Article
em En
| MEDLINE
| ID: mdl-844799
ABSTRACT
The binding between cholera toxin or its B-protein subunit and various ganglioside-related oligosaccharides was studied by equilibrium displacement dialysis. At low concentrations of ligand, the binding of monosialo-gangliotetraitol exceeded that of the parent ganglioside II3NeuAcGgOse4-Cer, the possible cell surface receptor for the toxin. The terminal galactose residue and an intact carboxyl group of the sialic acid moiety of monosialo-gangliotetraose were found to be necessary for strong binding to the toxin.
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Base de dados:
MEDLINE
Assunto principal:
Vibrio cholerae
/
Enterotoxinas
/
Gangliosídeos
Idioma:
En
Ano de publicação:
1977
Tipo de documento:
Article