Isolation of glucagon-37 (bioactive enteroglucagon/oxyntomodulin) from porcine jejuno-ileum. Characterization of the peptide

FEBS Lett. 1982 Sep 6;146(1):79-86. doi: 10.1016/0014-5793(82)80709-6.


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'.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Cell Membrane / analysis
  • Chemical Phenomena
  • Chemistry
  • Chromatography, High Pressure Liquid
  • Gastrointestinal Hormones / isolation & purification*
  • Glucagon-Like Peptides / isolation & purification*
  • Hydrolysis
  • Liver / analysis
  • Muscle, Smooth / analysis*
  • Oxyntomodulin
  • Radioimmunoassay
  • Swine


  • Amino Acids
  • Gastrointestinal Hormones
  • Oxyntomodulin
  • Glucagon-Like Peptides