Ahmad_2016_J.Environ.Biol_37_479

Acetylcholinesterase (AChE) from the brain tissue of local freshwater fish, Tor tambroides was isolated through affinity purification. Acetylthiocholine iodide (ATCi) was preferable synthetic substrate to purified AChE with highest maximal velocity (V(max)) and lowest biomolecular constant (K(m)) at 113.60 Umg(-1) and 0.0689 mM, respectively, with highest catalytic efficiency ratio (V(max)/K(m)) of 1648.77. The optimum pH was 7.5 with sodium phosphate buffer as medium, while optimal temperature was in the range of 25 to 35 degrees C. Bendiocarp, carbofuran, carbaryl, methomyl and propoxur significantly lowered the AChE activity greater than 50%, and the IC50 value was estimated at inhibitor concentration of 0.0758, 0.0643, 0.0555, 0.0817 and 0.0538 ppm, respectively.