Abstract
The catalytic efficiency of the field mouse ( Mus booduga) brain acetyl cholinesterase (AChE, EC 3.1.1.7) was significantly ( P < 0.001) decreased probably through the reduction in the active site density of the enzyme content and elevation in the activation energy (ΔE) requirements during repeated hexachlorophene (HCP) treatment. Fall in the activity potential of AChE may account for the interference of HCP or its reactive metabolites with the acetylcholine (ACh)-AChE system and deserve consideration in contributing to the neurotoxicity.
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