Structure and receptor-binding activity of insulin from a holostean fish, the bowfin (Amia calva)

J. M. Conlon, J. H. Youson, J. Whittaker

Research output: Contribution to journalArticlepeer-review

26 Citations (Scopus)

Abstract

The holostean fishes are the extant representatives of the primitive ray-finned fishes from which the present-day teleosts may have evolved. The primary structure of insulin from a holostean fish, the bowfin (Amia calva), was established as: A-chain: Gly-Ile-Val-Glu-Gln-Cys-Cys-Leu-Lys-Pro-Cys-Thr-Ile-Tyr-Glu-Met-Glu-Lys- Tyr-Cys-Asn; B-chain: Ala-Ala-Ser-Gln-His-Leu-Cys-Gly-Ser-His-Leu-Val-Glu-Ala-Leu-Phe-Leu-Val- Cys-Gly-Glu-Ser-Gly-Phe-Phe-Tyr-Asn-Pro-Asn-Lys-Ser. This amino acid sequence contains several substitutions (methionine at A16, phenylalanine at B16 and serine at B22) at sites that have been strongly conserved in other vertebrate species and that may be expected to influence biological activity. Consistent with this prediction, bowfin insulin was approx. 14-fold less potent than pig insulin in inhibiting the binding of [125I-Tyr-A14](human insulin) to transfected mouse NIH 3T3 cells expressing the human insulin receptor.

Original languageEnglish
Pages (from-to)261-264
Number of pages4
JournalBiochemical Journal
Volume276
Issue number1
DOIs
Publication statusPublished (in print/issue) - 1991

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