Purification and characterization of recombinant HspA-UreB fusion protein of Helicobacter pylori from inclusion body

Objective To establish an effective method for purificating recombinant HspA-UreB fusion protein of Helicobacter pylori from inclusion body. Methods The inclusion bodies of HspA-UreB fusion proteins expressed in recombinant E.coli BL21(pET-HU27) were washed, denatured and renatured. The fusion proteins were isolated and purified by A¨KTA Fast Protein Liquid Chromatogram(FPLC) with HiTrap Chelating HP, then the purity and content of target protein were detected by SDS-PAGE and Bradford method, and the immunocompetence was identified with Western blotting test. Results The recombinant HspA-UreB fusion protein from inclusion body was confirmed to have a purity and content of more than 90% and 0.25 g·L~ -1, respectively, and a high immunocompetence. Conclusion An effective method for purificating recombinant HspA-UreB fusion protein of Helicobacter pylori from inclusion body is established successfully.