Abstract
Acetylcholinesterase (AChE, E.C. 3.1.1.7) from an organophosphate-resistant strain of house fly, Musca domestica (L.) exhibited a decrease in sensitivity towards four organophosphates and two carbamates in comparison with enzyme from the parent susceptible strain. Sensitivity was less, as measured by the bimolecular reaction constant ( k i), by a factor of 117 for dichlorvos, 94 for paraoxon, 11 for diazoxon, 7 for Tetram, 62 for propoxur, and 50 for dimetilan. These differences in bimolecular reaction constants were attributed entirely to differences in their affinity for the enzyme, as measured by the dissociation constant, K d . It is suggested that the cross resistance to these inhibitors is due at least in part to insensitive acetylcholinesterase.
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