Primary structure of glucagon and a partial sequence of oxyntomodulin (glucagon-37) from the guinea pig

J. M. Conlon, H. F. Hansen, T. W. Schwartz

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34 Citations (Scopus)


Two glucagon-like peptides have been isolated from guinea pig pancreas and their primary structures determined. A 29-residue peptide is identical to the glucagons from all other mammals yet studied in the N-terminal region (residues 1-20) but the C-terminal region [Gln-Phe-Leu-Lys-Trp-Leu-Leu-Asn-Val] contains five substitutions. A 37-residue peptide probably represents guinea pig glucagon extended from the C-terminus by [Lys-Arg-Asn-Arg-Asn-Asn-Ile-Ala] and is analogous to human oxyntomodulin (glucagon-37). The structures suggest evolutionary pressure to conserve the N-terminal region of glucagon and the C-terminal region of oxyntomodulin. The biological activity of guinea pig glucagon has not yet been determined but it is speculated that changes in the C-terminal region of glucagon may have produced a molecule with reduced biological potency that is appropriate to the reduced potency of guinea pig insulin.

Original languageEnglish
Pages (from-to)309-320
Number of pages12
JournalRegulatory Peptides
Issue number4
Publication statusPublished - Aug 1985
Externally publishedYes


  • HPLC
  • hystricomorph
  • insulin
  • ion-exchange chromatography
  • radioimmunoassay

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Clinical Biochemistry
  • Cellular and Molecular Neuroscience


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