Inhibition of bovine serum acetylcholinesterase by in vitro exposure to malathion, malaoxon, isomalathion and diethyl maleate was investigated to elucidate the mechanism of the enzyme interaction with structurally similar organophosphorus compounds. IC50 (half maximum inhibitory concentrations) were determined by Hill analysis of experimentally obtained inhibition curves. The values (2.87 ± 0.24)x10-6 M, (2.65±0.61)x10-6M, (3.01±0.36)x10-4 M and (5.69 ±0.7)x10-2 M were obtained for malaoxon, isomalathion, malathion and their hydrolysis product diethyl maleate, respectively. The relationship between the structure of the compounds and their potency to inhibit the enzyme activity was discussed.Physical chemistry 2006 : 8th international conference on fundamental and applied aspects of physical chemistry; Belgrade (Serbia); 26-29 September 200
