The reactivation of cholinesterase inhibited with organophosphorus compounds. 1. Reactivation by 2-oxoaldoximes

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Abstract
Kinetic studies on the reactivation by 2-oxoaldoximes (R.CO.CH:N.OH) of cholinesterase inhibited with organophosphorus compounds show that the formation of a complex between the reactivator and the inhibited enzyme is a likely step in the reactivation process. Variation of the alkyl group (R) has only a minor effect on the reactivating power of 2-oxoaldoximes, which indicates that it is probably the carbonyl group in the oxoaldoxime which is linked to the enzyme in the complex. An explanation is given for the marked differences in reactivating powers of the isomeric pyridine hydroxamic acids.