Primary structure of insulin and glucagon from the flounder (Platichthys flesus)

J. Michael Conlon, Michael S. Davis, Lars Thim

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)


Insulin and glucagon have been isolated from the Brockmann bodies of the flounder, a teleostean fish, and their primary structures established by automated Edman degradation. The A-chain of flounder insulin shows strong homology to the A-chains from the coho salmon (Oncorhynchus kisutch; 100%) and the anglerfish (Lophius americanus; 95%) but homologies in the B-chain region are weaker (salmon 79%, anglerfish 83%). Flounder insulin B-chain contains the novel sequence Val-Val-Pro-Pro at the NH2 terminus and the highly conserved seryl residue at position 10 (B 9 in mammals) is replaced by an alanyl residue. Flounder glucagon is identical to anglerfish glucagon II but shows four amino acid substitutions compared with salmon glucagon.

Original languageEnglish
Pages (from-to)203-209
Number of pages7
JournalGeneral and Comparative Endocrinology
Issue number2
Publication statusPublished - May 1987
Externally publishedYes

ASJC Scopus subject areas

  • Animal Science and Zoology
  • Endocrinology


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