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 language | English |
|---|---|
| Pages (from-to) | 203-209 |
| Number of pages | 7 |
| Journal | General and Comparative Endocrinology |
| Volume | 66 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published (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 |
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| GRID 18097 |
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