Add time:08/16/2019         Source:sciencedirect.com

The inhibition of eel acetylcholinesterase by the 4-nitrophenyl esters of monochloromethyl(phenyl)-, dichloromethyl(phenyl)-, and phenyl(trichloromethyl)phosphinic acid (I, II, and III, respectively) was investigated at pH 6.90 in 0.067 M phosphate buffer (25.0°C) using stopped-flow instrumentation and automated data processing. The largest ki value (156,700 M−1 sec−1) was observed for the reaction of I with the enzyme. There is no direct relationship between the hydrolysis rates of the esters and their anticholinesterase activities on eel acetylcholinesterase. Spontaneous reactivation of the phosphinylated enzymes at pH 7.60 showed the following order of activity: I > III > II. The absence of aging is supported by oxime-induced reactivation studies.

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