Isolation of glucagon‐37 (bioactive enteroglucagon/oxyntomodulin) from porcine jejuno‐ileum

Abstract

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 ∼100%, 20% and 10%, respectively. In contrast, it is ∼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