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• W1988686670 abstract "Insulin was isolated from the pancreas of the American eel, Anguilla rostrata, and its primary structure was established as (Formula: see text). Eel insulin contains unusual substitutions at B-21, B-22, and B-26 in the putative receptor-binding region of the molecule compared with other mammalian and fish insulins. The A-chain of insulin from the European eel contains an asparagine rather than a serine residue at position A-12. Similarly, amino acid composition data indicate the B-chain of insulin from the European eel is appreciably different from that from the American eel. The primary structure of glucagon-like peptide (GLP) from the American eel is identical to that from the European eel, Anguilla anguilla. The primary structure of the peptide was established as (Formula: see text). Fast-atom bombardment mass spectrometry demonstrated that the COOH-terminal arginyl residue is alpha-amidated. The strong evolutionary pressure to conserve the structure of GLP provides further support for the assertion that the peptide plays an important regulatory role in teleost fish." @default.
• W1988686670 created "2016-06-24" @default.
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• W1988686670 date "1991-04-01" @default.
• W1988686670 modified "2023-10-14" @default.
• W1988686670 title "The primary structure of Glucagon-like peptide but not insulin has been conserved between the American eel, Anguilla rostrata and the European eel, Anguilla anguilla" @default.
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• W1988686670 doi "https://doi.org/10.1016/0016-6480(91)90292-e" @default.
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