In the present study, the prokaryotic expression of glutathione transferase (GST) gene from Taenia solium and its immunological properties were investigated by means of biological informatics methods. The GST gene from T.solium was screened from the cDNA plasmid library of the adult worms. This gene was cloned into prokaryotic expression plasmid pET28a(+) and then expressed in E.coli BL21(DE3) after double enzyme digestion, PCR identification and IPTG induction. The expressed product was identified by SDS-PAGE and the recombinant protein was purified through purification column of His-Ni~(2+) protein. Meanwhile, the immunoreactivity of the purified protein was analyzed by Western blot assay. In these ways, the recombinants were successfully constructed and the highly purified proteins were obtained. It was demonstrated that these proteins could be recognized by sera of patients infected with T.asitica and T.rhynchus saginatus. From these observations, it is evident that highly efficient expression of GST of Taenia solium with definite immunoreactivity can be demonstrated in the prokaryotic expression system.