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. 1987 Aug 1;245(3):851–855. doi: 10.1042/bj2450851

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

J M Conlon 1, E Dafgård 1, S Falkmer 1, L Thim 1
PMCID: PMC1148206  PMID: 3311036

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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