Abstract
This paper constitutes the first report on the spontaneous reactivation of a cholinesterase following inhibition by an organophosphinate. The spontaneous reactivation of eel acetylcholinesterase following inhibition by p-nitrophenyl diphenylphosphinate (DPP), p-nitrophenyl methyl(phenyl)phosphinate (MPP), and p-nitrophenyl dimethylphosphinate (DMP) at 25.0°C in 0.10 M 3-( N-morpholino)propanesulfonic acid buffer of pH 7.60 reflected the following order of activity: MPP > DPP > DMP. Hydrolysis studies of the phosphinate esters under these conditions exhibited the same order of reactivity. Kinetic studies on the spontaneous reactivation of methyl(phenyl)phosphinylated eel acetylcholinesterase at pH 7.60 and pH 9.10 showed a 100% recovery of enzymatic activity, thus demonstrating the absence of aging. The absence of aging was further supported by oxime-induced reactivation studies.
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