Isolation of glucagon-37 (bioactive enteroglucagon/oxyntomodulin) from porcine jejuno-ileum. Characterization of the peptide.
A peptide isolated from porcine gut according to its glucagon-like activity in liver (bioactive enteroglucagon) has been characterized immunologically, biologically and chemically: its potency relative to pancreatic glucagon in interacting with an antiglucagon antibody, hepatic glucagon-binding sites and hepatic adenylate cyclase was approximately 100%, 20% and 10%, respectively. In contrast, it is approximately 20-times more potent than glucagon in oxyntic glands, justifying the term 'oxyntomodulin'. Chemically, it consists in the 29 amino acid-peptide glucagon elongated at its C-terminal end by the octapeptide Lys-Arg-Asn-Lys-Asn-Asn-Ile-Ala; accordingly, it is called 'glucagon-37'.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002462:Cell Membrane / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D002851:Chromatography, High Pressure Liquid; D005768:Gastrointestinal Hormones / Q000302:isolation & purification*; D004763:Glucagon-Like Peptides / Q000302:isolation & purification*; D006868:Hydrolysis; D008099:Liver / Q000032:analysis; D009130:Muscle, Smooth / Q000032:analysis*; D053772:Oxyntomodulin; D011863:Radioimmunoassay; D013552:Swine
D000596:Amino Acids; D005768:Gastrointestinal Hormones; D053772:Oxyntomodulin; D004763:Glucagon-Like Peptides