Phosphinate inhibition studies of cholinesterases

Abstract

AbstractThe kinetic constants, Kd, k2, and ki, were determined for the inhibition by 4‐nitro‐phenyl methyl(phenyl)phosphinate of three cholinesterases: butyrylcholinesterase, bovine erythrocyte acetylcholinesterase and eel acetylcholinesterase. Stopped‐flow kinetic evaluations and automated data acquisition and processing were employed. A broad range in affinity for the phosphinate inhibitor was observed as reflected by the binding constants, Kd. A similar wide range in the k2 values for the unimolecular inhibition step was obtained. The net bimolecular rate constants, ki, indicate equal overall reactivity for butyrylcholinesterase and eel acetylcholinesterase with a smaller inhibition rate constant for bovine erythrocyte acetylcholinesterase.