In vitro studies on the reactivation by oximes of phosphylated acetylcholinesterase—I: On the reactions of P2S with various organophosphates and the properties of the resultant phosphylated oximes

Abstract The rates of formation and decomposition of a series of phosphylated oximes derived from P2S (2-hydroxy-iminomethyl-1-methylpyridinium methane-sulphona have been measured. The rates of inhibition of AChE by these phosphylated oximes and the parent (and related) organosphosphates have also been measured. Possession of these rate data now permits a detailed analysis of the reactivation of phosphylated AChE by P2S to be made (see following paper).