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Catalytic activity of acetylcholinesterase (AChE; EC 3.1.1.7) was studied in the presence of oximes HI-6, K114, K127 and K203, and inhibition constants were determined for the reversible enzyme–inhibitor complex (K I ). Based on the mixed inhibition model, inhibition constants were 0.020mM for HI-6, 0.0021mM for K114, 0.175mM for K127, and 0.036mM for K203. Molecular modelling of AChE–oxime...
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