A glucagon-like peptide, structurally related to mammalian oxyntomodulin, from the pancreas of a holocephalan fish, Hydrolagus colliei

Biochem J. 1987 Aug 1;245(3):851-5. doi: 10.1042/bj2450851.


The pancreatic islets of the holocephalan fishes contain, in addition to A-, B- and D-cells, X-cells, which are immunoreactive towards antisera directed against the N-terminal region of glucagon but not towards antisera directed against the C-terminal region. A 36-amino-acid-residue peptide was isolated from the pancreas of a holocephalan fish, the Pacific ratfish (Hydrolagus colliei), that shows homology (69%) to mammalian glucagon in its N-terminal region and is reactive towards an N-terminally directed antiserum. Reactivity towards C-terminally directed antisera is prevented by the presence of a 7-residue C-terminal extension to the glucagon sequence that shows limited homology to the C-terminal region of glucagon-37 (oxyntomodulin). It is proposed that this peptide represents a major storage product of the islet X-cell.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acids / analysis
  • Animals
  • Chromatography, Gel
  • Chromatography, High Pressure Liquid
  • Fishes / metabolism*
  • Glucagon / immunology
  • Glucagon-Like Peptides
  • Islets of Langerhans / analysis*
  • Peptides / analysis


  • Amino Acids
  • Peptides
  • Glucagon-Like Peptides
  • glucagon-like-immunoreactivity
  • Glucagon