Expression and purification of recombinant interferon-gamma

Objective To research interferon-gamma expression and purification methods in E.coli and provide experimental basis for further lots of production. Methods Using DNA recombinant technology,IFN-γ cDNA,which reversed transcription from Chinese lymphocyte mRAN, was cloned to the prokaryotic expression plasmid pBV220 and was constructed pBVIFN of efficient expression vector, then transferred into E.coli plyass.IFN-γ can be expressed efficiently by termoinduction. By the inclusion bodies dissolution, renaturation,concentration and DEAE ion exchange chromatography IFN-γ was purified. Results The IFN-γ expression yield was 40 4% of bacterial soluble proteins. The purification of the inclusion bodise was 70%. The total biological activity was 1 27×10 9 U.The specific activity was 1 31×10 9 U/L.The activity recovery rate was 77.7%. Conclusion The experiment method will lay a foundation for lots of production of the interferon-gamma.