Formation of native insulin from the scrambled molecule by protein disulphide-isomerase.

Formation of native insulin from the scrambled molecule by protein disulphide-isomerase.
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通过蛋白质二硫键异构酶从乱序分子形成天然胰岛素。

DOI:
10.1042/bj2550451
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发表时间:
1988
期刊:
The Biochemical journal
影响因子:
--
通讯作者:
Tsou,CL
Tsou,CL
中科院分区:
--
文献类型:
--
作者:
Tang,JG;Wang,CC;Tsou,CL

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通过蛋白质二硫化物异构酶从乱序胰岛素或从分离的A链和B链S-磺酸盐形成天然胰岛素,经高效液相色谱测定,产率为20-30%。分析、受体结合和刺激脂肪生成。H.P.L. C反应产物的分布图显示,在所有可能的含有两条链的异构体中,天然激素是迄今为止占主导地位的产物,因此在某些条件下最稳定。
The formation of native insulin either from scrambled insulin or from the separated A chain and B chain S-sulphonates by protein disulphide-isomerase was demonstrated with yields of 20-30% as measured by h.p.l.c. analysis, receptor binding and stimulation of lipogenesis. The h.p.l.c. profile of the reaction products shows that, among all the possible isomers containing both chains, the native hormone is by far the predominating product and consequently the most stable under certain conditions.
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