Carbamylation and binding constants for the inhibition of acetylcholinesterase by physostigmine (eserine)

Abstract

The kinetic treatment and experimental procedures which have been used to evaluate the binding and phosphorylation rate constants of organophos phate inhibitors were applied to the carbamate inhibitor eserine. The binding constant K(I)carbamylation rate constant k(2e)for the inhibition of acetyl cholinesterase by eserine were successfully evaluated.