The reactivation of cholinesterase inhibited with organophosphorus compounds. 2. Reactivation by pyridinealdoxime methiodides

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Abstract
Kinetic studies of reactivation by pyridine-2- and -4-aldoxime methiodides of erythrocyte cholinesterase inhibited with organophosphorus compounds indicate that a preliminary step is the formation of a complex between the inhibited enzyme and the reactivator. The reactivating powers of the isomeric pyridinealdoxime methiodides are compared in terms of their intrinsic reactivities with organophosphorus inhibitors, the strength of the complexes and the orientation of the reactivator in the complex.