Isolation from chicken antrum, and primary amino acid sequence of a novel 36-residue peptide of the gastrin/CCK family.
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.
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens / Q000235:genetics / Q000378:metabolism*; D002766:Cholecystokinin / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D003429:Cross Reactions; D005755:Gastrins / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification; D010455:Peptides / Q000235:genetics / Q000276:immunology / Q000302:isolation & purification*; D011706:Pyloric Antrum / Q000032:analysis*; D012689:Sequence Homology, Nucleic Acid; D013045:Species Specificity; D013552:Swine / Q000235:genetics / Q000378:metabolism
D005755:Gastrins; D010455:Peptides; D002766:Cholecystokinin