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.
The rates of formation and decomposition of a series of phosphylated oximes derived from P2S (2-hydroxy-iminomethyl-1-methylpyridinium methane-sulphonate) have been measured. The rates of inhibition of AChE by these phosphylated oximes and the parent (and related) organophosphates 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).
D000110:Acetylcholinesterase; D000818:Animals; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D002800:Cholinesterase Inhibitors / Q000037:antagonists & inhibitors*; D002801:Cholinesterase Reactivators; D007700:Kinetics; D009943:Organophosphorus Compounds / Q000037:antagonists & inhibitors*; D010091:Oximes; D014867:Water
D002800:Cholinesterase Inhibitors; D002801:Cholinesterase Reactivators; D009943:Organophosphorus Compounds; D010091:Oximes; D014867:Water; D000110:Acetylcholinesterase