银鲛胰岛素的一级结构揭示了胰岛素原加工的一种不同寻常的模式。

The primary structure of ratfish insulin reveals an unusual mode of proinsulin processing.

作者信息

Conlon J M, Dafgård E, Falkmer S, Thim L

出版信息

FEBS Lett. 1986 Nov 24;208(2):445-50. doi: 10.1016/0014-5793(86)81066-3.

DOI:10.1016/0014-5793(86)81066-3

Abstract

The primary structure of insulin from the Holocephalan fish, Hydrolagus colliei (the ratfish), has been established by automated Edman degradation as: (Formula: see text). The presence of a COOH-terminal extension to the B-chain is consistent with the occurrence of a single base mutation in the region of the gene encoding one of the dibasic residue processing sites [Arg31(AGA)----Ile* (AUA)] with the result that the ratfish has utilised an alternative cleavage site within the C-peptide region of proinsulin.

摘要

银鲛目鱼类——银鲛（兔银鲛）胰岛素的一级结构已通过自动Edman降解法确定为：（分子式：见正文）。B链存在COOH末端延伸，这与编码双碱性残基加工位点之一的基因区域发生单个碱基突变[精氨酸31（AGA）→异亮氨酸*（AUA）]的情况一致，结果是兔银鲛利用了胰岛素原C肽区域内的另一个切割位点。

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引用本文的文献

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A glucagon-like peptide, structurally related to mammalian oxyntomodulin, from the pancreas of a holocephalan fish, Hydrolagus colliei.一种与哺乳动物胃动素结构相关的胰高血糖素样肽，来自全头亚纲鱼类银鲛的胰腺。

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