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

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Abstract

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
Volume66
Issue number2
DOIs
Publication statusPublished (in print/issue) - May 1987

Funding

This work was supported by the Stiftung Vofks-wagenwerk and SERC (UK) Grant GRID 18097. The authors thank Professor N. Hilschmann, Max-Planck-Institut fiir Experimentelle Medizin, Giittingen, for providing facilities for amino acid analysis.

Funder number
GRID 18097

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