Isolation and Characterization of Chicken Secretin

Publisher Website
Google Scholar
Abstract
Chicken secretin was isolated and its structure determined. It is composed of 27 amino acid residues and has an amidated C terminus. The amino acid sequence is His-Ser-Asp-Gly-Leu-Phe-Thr-Ser-Glu-Tyr-Ser-Lys-Met-Arg-Gly-Asn-Ala-Gln-Val-Gln-Lys-Phe-Ile-Gln-Asn-Leu-Met-NH2. The structure shows distinct similarities to porcine secretin; amino acid identities occur at 14 positions (residues 1-4, 6-9, 11, 14, 17, 20, 24 and 26) but considerable differences are present among the remaining 13 positions. Chicken secretin further shows a clear structural similarity to the vasoactive intestinal peptide (37% identical positions), the gastric inhibitory peptide (30% identical positions) and to glucagon (52% identical positions), suggesting wide evolutionary and functional relationships.