[Extraction and characterization of a gastrosecretagogue peptide from the pancreas (author's transl)]

Abstract

A peptide which stimulates gastric acid secretion in the rat has been isolated from the normal porcine pancreas. It consists of 13 amino acids and has a molecular weight of 1286. It has been named GSP (gastrosecretagogue pancreatic peptide) on account of its main biological activity. Although its influence on gastric acid secretion is gastrin-like, there are marked biochemical and immunological differences between gastrin and GSP. The two substances are separable from each other by Sephadex gel filtration, by ion-exchange chromatography, and by disc electrophoresis. Furthermore, there are differences in the UV-absorption spectrum and in the amino acid composition. GSP does not react with gastrin antibodies in a radioimmunological system. GSP is considered to be a new polypeptide hormone by means of which the pancreas plays a role in the regulation of gastric acid secretion.