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

FEBS Letters

Gregory, H.¹  Dimaline, R.²  Young, J.¹ 

[1] MRC Secretory Control Group, Physiological Laboratory, University of Liverpool, PO Box 147, Liverpool L69 3BX England;Imperial Chemical Industries PLC, Mereside Alderley Park, Macclesfield SK10 4TG, England

关键词: Amino acid sequence Antrat peptide Tryptic digestion HPLC Gastrin Cholecystokinin;   

DOI  :  10.1016/0014-5793(86)80920-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown