Paper Report for: Harvey_1986_Biochem.Pharmacol_35_737
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Title: 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 Harvey B, Scott RP, Sellers DJ, Watts P Ref: Biochemical Pharmacology, 35:737, 1986 : PubMed
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).
        
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Harvey B, Scott RP, Sellers DJ, Watts P (1986) 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 Biochemical Pharmacology35: 737-44
Harvey B, Scott RP, Sellers DJ, Watts P (1986) Biochemical Pharmacology35: 737-44