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将人胰岛素原突变体（Ａ４Ｇｌｕ→Ｌｅｕ）基因重组到ｐＢＶ２２０表达载体上，在Ｅ．ｃｏｌｉ系统中得到高效表达，表达产物经ＳｅｐｈａｄｅｘＧ－５０柱层析分离以及胰蛋白酶和羧肽酶Ｂ的酶促转化等步骤，可得到纯的人胰岛素突变体（Ａ４Ｇｌｕ→Ｌｅｕ），其氨基酸组成与预期值相符，其受体结合活性及生物活性与标准猪胰岛素的基本相同。
The human proinsulin mutant (A4Glu → Leu) gene was recombined into pBV220 expression vector and expressed in E.coli. coli system was highly expressed, the expression product was separated by SephadexG-50 column chromatography and enzymatic conversion of trypsin and carboxypeptidase B and other steps can be obtained pure human insulin mutant (A4Glu → Leu), the amino acid composition and Expected value consistent with its receptor binding activity and biological activity of the standard porcine insulin is basically the same.