The high-throughput screening system for inhibitor mycobacterium tuberculosis compounds based on atp hydrolysis activity of recombinant protein ClpC1

The steady-state growth of recombinant ClpC1 protein in Luria-Bertani (LB) broth High Salt medium was maintained and stabilized after extraction. The determined ATPase activity of ClpC1 was performed by measuring the released phosphate from the reaction. Ecumicin was chosen to be a control compound with expected ATP hydrolysis activities (Hill coefficient = 1,19 ± 0,217; Kd value = 0,52 ± 0,275).