在大肠杆菌温度诱导体系中以非融合方式进行去Ｂ链羧端七肽人胰岛素原基因的表达，获得去Ｂ链羧端七肽人胰岛素原，表达产物占细胞总蛋白量的１３％，表达产物经ＳｅｐｈａｄｅｘＧ－５０柱层析分离及胰蛋白酶和羧肽酶Ｂ的酶促转化等步骤，可得到纯度达９４％以上的去Ｂ链羧端七肽人胰岛素，其氨基酸组成与预期值相符，受体活性是标准猪胰岛素的１％． Expression of human proinsulin gene of B-terminal carboxyheptamer in Escherichia coli temperature induction system was carried out in a non-fusion manner, and the human proinsulin to B chain carboxylase terminal peptide was obtained. The expression product accounted for 13% of the total cellular protein, The product was purified by SephadexG-50 column chromatography and enzymatic conversion of trypsin and carboxypeptidase B and other steps to obtain the purity of more than 94% of the B chain carboxylated heptasaponin human insulin, amino acid composition and expected value, Receptor activity is 1% of standard porcine insulin.