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Title: Primary structure of insulin and glucagon from the flounder (Platichthys flesus). Author: Conlon JM, Davis MS, Thim L. Journal: Gen Comp Endocrinol; 1987 May; 66(2):203-9. PubMed ID: 3556313. 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.[Abstract] [Full Text] [Related] [New Search]