Journal article

IDENTIFICATION OF A GASTRIN BINDING-PROTEIN IN PORCINE GASTRIC-MUCOSAL MEMBRANES BY COVALENT CROSS-LINKING WITH IODINATED GASTRIN-2, GASTRIN-17

GS BALDWIN, R CHANDLER, DB SCANLON, J WEINSTOCK

JOURNAL OF BIOLOGICAL CHEMISTRY | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | Published : 1986

Abstract

A gastrin binding protein (GBP) has been identified in detergent extracts of porcine gastric mucosal membranes by covalent cross-linking to 125I-[Nle15]gastrin with disuccinimidyl suberate. The apparent molecular weight of the cross-linked complex (80,000) is uneffected by reduction suggesting that the GBP is not composed of disulfide-bonded subunits. Subtraction of the molecular weight of 125I-gastrin indicates that the molecular weight of the GBP is 78,000. A similar molecular weight has been observed previously for the gastrin receptor (74,000) on intact canine parietal cells and plasma membranes therefrom, and for the receptor for the related hormone cholecystokinin (76,000-85,000) on pa..

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