Expression and Identification of Phosphoglucomutase Gene of Brucella

To express pgm fusion protein in E.coli BL21 and purify and identify the expressed product,so as to provided the material basis for the study of the function of the gene.The full-length pgm gene was synthesized by PCR and cloned into vector pET-28a(+).The constructed recombinant plasmid pET-pgm was transformed to competent E.coli BL21 expression under induction of IPTG.The expressed protein was purified with Ni-NTA Agarose,identified by Western blot,and the full-length pgm gene was sequenced.Both restriction analysis and sequencing proved that recombinant plasmid pET-pgm was constructed correctly.The SDS-PAGE and western blot analysis indicated that the recombinant protein induced by IPTG was about 64 ku.The protein can produce specific binding reaction,and has a good immune response with Brucella sera.