| Objective Tuberculosis is the leading cause of death in the entire world due to infection with a single microorganism at present. Looking for novel anti-tubercular gene target, research and development of drugs with new mechanisms of action, especially new agents with activity against pathogen of human latency are crucial tasks of present study. We chose the key enzyme of the Mycobacterium tuberculosis metabolic pathway as an original target for the new drugs research and development. To obtain recombinant protein with enzymatic activities of Isocitrate Lyase (ICL). Methods The icl gene was amplified by Polymerase Chain Reaction (PCR) from M. tuberculosis H37Rv strain genomic DNA and cloned into pET28-a (+) vector. The recombinant protein was expressed in E.coli BL21 (DE3). The characteristics of the recombinant enzyme was assayed after it was purified with Ni-NTA resin. Results The enzymatic properties demonstrated the purified recombinant protein had activities of ICL. The recombinant ICL was purified in a highly active state with a specific activity of about 7.657×102 umol.mg-1min-1. The pH curve indicates that recombinant ICL activity optimal at pH 7.4. The LC/MS spectrometry gave a 50603.347Da molecular mass of recombinant ICL. The CD spectrum showed that the...
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