蛋白质二硫键异构酶将无序分子转化为天然胰岛素。
Formation of native insulin from the scrambled molecule by protein disulphide-isomerase.
作者信息
Tang J G, Wang C C, Tsou C L
机构信息
Institute of Biophysics, Academia Sinica, Beijing, China.
出版信息
Biochem J. 1988 Oct 15;255(2):451-5. doi: 10.1042/bj2550451.
Abstract
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.
摘要
通过蛋白质二硫键异构酶从混乱的胰岛素或从分离的A链和B链S-磺酸盐形成天然胰岛素得到了证实，通过高效液相色谱分析、受体结合和脂肪生成刺激测定，产率为20%-30%。反应产物的高效液相色谱图谱表明，在所有包含两条链的可能异构体中，天然激素是迄今为止占主导的产物，因此在某些条件下是最稳定的。
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Resynthesis of insulin from its glycyl and phenylalanyl chains.从胰岛素的甘氨酰链和苯丙氨酰链重新合成胰岛素。
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