[Application of a gel chromatography renaturing way on low molecular single-chain urokinase mutant(DscuPA-32K)]

A recombinant mutant gene with thrombolytic and antithrombolytic bifunction was expressed in E. coli. Owing to two reasons of high molecular weight and over expression, dscuPA existed in inclusion body form. The protein of inclusion body was inactive protein. In order to obtain active protein, inclusion bodies should be denatured and then renatured. We performed a novel way named gel-chromatography column renaturation way. Compare with traditional renaturation way, this refolding approach had some obvious advantages, such as low cost and high recovery, and accomplished the preliminary purification step of desired protein(DscuPA-32K). Especially to proteins that easily became inactive and degradation, this approach might have good prospect.