Cloning and characterization of β-carbonic anhydrase, a potential drug target of Schistosoma japonicum

Zhongguo xue xi chong bing fang zhi za zhi = Chinese journal of schistosomiasis control
Zhang Cong-Hui, Zhu Huai-Min

Abstract

To express the beta carbonic anhydrase (β-CA) of Schistosoma japonicum, and analyze its catalytic activity. The cDNA and amino sequence which may encode β-CA of S. japonicum were obtained by the bioinformatics-method, and then the cDNA sequence was cloned into prokaryotic expression vector pET-32a (+) and expressed. After examining by SDS-PAGE and Western blotting, the recombinant protein was purified by Ni-affinity chromatography and the catalytic activity was determined. The sequence Sjp_0056790.1 took on the conservative position of β-CAs. The PCR and restriction enzyme digestion confirmed the construction of recombinant plasmid pET-32a (+) -SjaCA. SDS-PAGE and Western blotting analyses showed that the molecular weight of recombinant protein was about 38 kDa as expected, and it could be recognized by anti-His tag antibody. The catalytic activity determining revealed that the recombinant protein SjaCA owned the carbonic anhydrase activity. Sjp_0056790.1 encodes the β-CA of S. japonicum, and the β-CA with catalytic activity is successfully expressed, so it lays a foundation for the subsequent research of pharmacological inhibition, providing theoretic basis for searching and developing a new feasible anti-schistosome drug.

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