Isolation from chicken antrum, and primary amino acid sequence of a novel 36‐residue peptide of the gastrin/CCK family

15 September 1986

journal article
research article
Published by Wiley in FEBS Letters

Vol. 205 (2) , 318-321
https://doi.org/10.1016/0014-5793(86)80920-6

Abstract

A peptide that cross-reacted with C-terminal gastrin/CCK antisera was isolated from chicken antral extracts by a combination of gel filtration and reversed-phase HPLC. The sequence was: Phe-Leu-Pro-His-Val-Phe-Ala-Glu-Leu-Ser-Asp-Arg-Lys-Gly-Phe-Val-Gln-Gly-Asn-Gly-Ala-Val-Glu-Ala-Leu-His-Asp-His-Phe-Tyr-Pro-Asp-Trp-Met-Asp-Phe(NH₂). Aside from the C-terminal tetrapeptide and the Tyr residue, the molecule does not resemble other known forms of gastrin or CCK. The peptide was a potent stimulus of avian gastric acid but not pancreatic secretion. The results have important implications for the structure-activity and evolutionary relationships of the gastrin/CCK family.

Keywords

AMINO ACID SEQUENCE ANTRAT PEPTIDE TRYPTIC DIGESTION HPLC GASTRIN CHOLECYSTOKININ

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