title: Isolation and characterization of chicken secretin.
abstract: Chicken secretin has been 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 that of 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 also 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.
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D002918:Chymotrypsin; D004386:Duodenum / Q000032:analysis; D005749:Gastric Inhibitory Polypeptide; D005934:Glucagon; D007583:Jejunum / Q000032:analysis; D012633:Secretin / Q000302:isolation & purification*; D013045:Species Specificity; D013552:Swine; D014357:Trypsin; D014422:Turkeys; D014660:Vasoactive Intestinal Peptide
chemical_list: D012633:Secretin; D014660:Vasoactive Intestinal Peptide; D005749:Gastric Inhibitory Polypeptide; D005934:Glucagon; D002918:Chymotrypsin; D014357:Trypsin