title: Structure and receptor-binding activity of insulin from a holostean fish, the bowfin (Amia calva).
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.
authors.affiliation: Department of Biomedical Sciences, Creighton University Medical School, Omaha, NE 68178.
authors.forename: J M
authors.initials: JM
authors.lastname: Conlon
authors.forename: J H
authors.initials: JH
authors.lastname: Youson
authors.forename: J
authors.initials: J
authors.lastname: Whittaker
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001667:Binding, Competitive; D002460:Cell Line; D002851:Chromatography, High Pressure Liquid; D005260:Female; D005399:Fishes; D007328:Insulin / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D046911:Macromolecular Substances; D008297:Male; D051379:Mice; D008969:Molecular Sequence Data; D011972:Receptor, Insulin / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D013552:Swine
chemical_list: D007328:Insulin; D046911:Macromolecular Substances; D011972:Receptor, Insulin