Structure and receptor-binding activity of insulin from a holostean fish, the bowfin (Amia calva).
Structure and receptor-binding activity of insulin from a holostean fish, the bowfin (Amia calva).
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来自全骨鱼弓鳍鱼（Amia calva）的胰岛素的结构和受体结合活性。
DOI：
10.1042/bj2760261
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Whittaker,J
中科院分区：
文献类型：
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作者：
Conlon,JM;Youson,JH;Whittaker,J
海龙鱼是现存的原始鳍鱼的代表，今天的硬骨鱼可能就是从这些鱼进化而来的。一种全骨鱼类弓鳍(Amia Calva)的胰岛素的一级结构，确定为：A链：Gly-Ile-Val-Glu-Gln-Cys-Cys-Leu-Lys-Pro-Cys-Thr-Ile-Tyr-Glu-Met-Glu-赖氨酸-酪氨酸-半胱氨酸-天冬氨酸B链：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该氨基酸序列包含几个取代基(A16位的蛋氨酸，B16的苯丙氨酸和B22的丝氨酸)在其他脊椎动物物种中高度保守的位置，可能会影响生物活性。与这一预测相一致的是，鲍芬胰岛素大约是。在抑制[125I-Tyr-A14](人胰岛素)与表达人胰岛素受体的转基因小鼠NIH 3T3细胞的结合方面，其效力比猪胰岛素低14倍。
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.