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将人工全化学合成的尿激酶原（ｐｒｏ－ｕｒｏｋｉｎａｓｅ）ｃＤＮＡ克隆到表达载体ｐＥＴ３ｄ中，转化大肠杆菌ＢＬ２１（ＤＥ３）ＬｙｓＳ，经ＩＰＴＧ诱导，获得了占菌体总蛋白１８％的高表达。经ＳＤＳ－ＰＡＧＥ和Ｗｅａｔｅｒｎ－ｂｌｏｔ鉴定，表达产物主要为单链尿激酶，并且在菌体内基本以无活性的包涵体形式存在。经体外交复性，从１Ｌ培养基中可获得３０００００单位的活性原激酶原。
The artificial full chemical synthesized pro-urokinase cDNA was cloned into the expression vector pET3d and transformed into E. coli BL21 (DE3) LysS. After induced by IPTG, the prokaryotic expression protein accounted for 18% of total bacterial proteins. The results of SDS-PAGE and Weatern-blot showed that the expressed product was predominantly single-chain urokinase and existed in the body as an inactive inclusion body. After in vitro healing, 300000 units of active pro-kininogen can be obtained from 1L of culture medium.