Add time:08/17/2019         Source:sciencedirect.com

The inhibition of eel acetylcholinesterase and bovine erythrocyte acetylcholinesterase by the 4-nitrophenyl esters of methyl-, ethyl-, and isopropyl(phenyl)phosphinic acid (MPP, EPP, and IPP, respectively) was investigated at pH 6.90 in 0.067 M phosphate buffer (25.0°C) using stopped-flow instrumentation and automated data processing. Our evaluation of the dissociation constant, Kd, the unimolecular bonding rate constant, k2, and the bimolecular reaction constant, ki, are the first reported values for these constants for a homologous series of this class of organophosphorus compounds. The largest k1 value (29,428 M−1 sec−1) was observed for the reaction of eel acetylcholinesterase with 4-nitrophenyl methyl(phenyl)phosphinate. The smallest ki value (9.6 M−1 sec−1) was observed for the reaction of bovine erythrocyte acetylcholinesterase with 4-nitrophenyl isopropyl(phenyl)phosphinate.

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