B_(23)-Gly-B_(24)人胰岛素的分离纯化及性质研究

Purification and Characterization of B_23-Gly-B_24 Human Insulin

为了研究胰岛素B链羧端的自由度对于胰岛素与受体相互作用的影响。在人胰岛素B链羧端（转角区回折点B23与B24之间插入一个Gly。B23-Gly-B24人胰岛素原在大肠杆菌的表达产物占细胞总蛋白量的28％,B23-Gly-B24人胰岛素的受体活性分别是标准猪胰岛素的122％和人胰岛素的111％。说明以较高的受体结合活性获得了高纯度的B23-Gly-B24人胰岛素。

In order to study the effect of increased flexibility of C-terminal of insulin B chain on its receptor binding activity, a Gly was inserted between B23 and B24, of insulin B chain β turn in hope of providing more flexibility to its C terminal. The expression level of 823-Gly-B24 Human prolnsulin accounted for 28% of total bacterial proteins. B23-Gly-B24 human insulin's receptor binding activity is 122% as compared with standard porcine insulin. Purified B23-Gly-B24 Human Insulin was obtained by the common methods and it's receptor binding activity was high.