[High-level expression of human acidic fibroblast growth factor in E. coli and its purification]

A reconstructed human acidic fibroblast growth factor (haFGF) cDNA was cloned into the expression vector pkk223-3, and the expression in Escherichia coli. JM109 was induced by IPTG induction; the expression level of the recombinant haFGF was about 80 mg/L. The expressed haFGF was purified to identity by heparin affinity chromatography and the recovery rate of haFGF was 65%. The specific activity of the purified haFGF was ED50 4.6 ng/ml. The characters of recombinant haFGF was identical to that of natural one.