Structure and function of insulin: preparation and biological activity of guinea pig des B-Asp30,des-A-Asn21-insulin.
Structure and function of insulin: preparation and biological activity of guinea pig des B-Asp30,des-A-Asn21-insulin.
复制标题
胰岛素的结构与功能：豚鼠des B-Asp30、des-A-Asn21-胰岛素的制备及其生物活性。
DOI：
10.1139/o76-124
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发表时间：
1976
期刊：
影响因子：
--
通讯作者：
M. Moule
中科院分区：
文献类型：
--
作者：
C. Yip;M. Moule
以牛胰岛素和豚鼠胰岛素为原料，经羧肽酶A （EC 3.4.12.2）消化制备牛des-B-Ala30、des-A- asn21 -胰岛素和豚鼠des-B-Asp30、des-A- asn21 -胰岛素。据其他研究者报道，牛des-Ala30、des- asn21 -胰岛素的生物活性低于牛胰岛素的10%。与理论考虑相反，从豚鼠胰岛素的碳基末端去除a - asn21和B-Asp30导致90%以上的生物活性丧失。这些胰岛素衍生物的受体结合研究表明，生物活性的丧失与结合亲和力的降低之间存在良好的相关性。提示胰岛素的羧基末端A-Asn21可能直接与胰岛素受体相互作用。
Bovine des-B-Ala30,des-A-Asn21-insulin and guinea pig des-B-Asp30,des-A-Asn21-insulin were prepared from bovine and guinea pig insulin by digestion with carboxypeptidase A (EC 3.4.12.2). As reported by other investigators, the biological activity of bovine des-Ala30,des-Asn21-insulin was less than 10% that of bovine insulin. Contrary to theoretical consideration, removal of A-Asn21 and B-Asp30 from the carbosyl termini of guinea pig insulin resulted in a loss of more than 90% of the biological activity. Receptor binding studies of these insulin derivatives demonstrated a good correlation between the loss of biological activity and the decrease in binding affinity. It is suggested that the carboxyl terminal A-Asn21 of insulin may interact directly with the insulin receptor.