Lectin binding to the porcine and human ileal receptor of intrinsic factor-cobalamin.
Fiche publication
Date publication
janvier 1989
Journal
Glycoconjugate journal
Auteurs
Membres identifiés du Cancéropôle Est :
Pr GUEANT Jean-Louis, Pr SCHOHN Hervé
Tous les auteurs :
Jokinen O, Guéant JL, Schohn H, Gräsbeck R
Lien Pubmed
Résumé
The purified porcine receptor for the intrinsic factor-cobalamin complex bound to concanavalin A, lentil lectin and wheat germ lectin covalently coupled to Sepharose and was eluted with the corresponding soluble sugars. In contrast, human intrinsic factor bound efficiently to concanavalin A, to some extent to lentil lectin, but only slightly to wheat germ agglutinin. The binding of IF-Cbl to the receptor was inhibited when the receptor was pre-incubated with soluble wheat germ agglutinin, with an inhibition constant estimated to be 1.9 mumol/l. After transfer of the purified receptor from SDS-PAGE to Immobilon, ligand blotting of the purified receptor with iodinated lectin showed that concanavalin A and lentil lectin bound to three (75, 56 and 43 kDa) components but that wheat germ agglutinin bound only to the 75 kDa component. These results showed that the alpha subunit of the receptor could bind to wheat germ agglutinin, resulting in an inhibition of its binding with intrinsic factor. Both binding sites of intrinsic factor and of wheat germ agglutinin could be located near to each other.
Mots clés
Animals, Chromatography, Affinity, Chromatography, Gel, Electrophoresis, Polyacrylamide Gel, Humans, Ileum, Intestinal Mucosa, metabolism, Intrinsic Factor, isolation & purification, Kinetics, Lectins, Molecular Weight, Receptors, Cell Surface, isolation & purification, Receptors, Peptide, Swine, Vitamin B 12, metabolism
Référence
Glycoconj. J.. 1989 ;6(4):525-38