The effect of alcohols on cholinesterase

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Abstract
Alcohols were found to bring about activation of the enzyme up to an optimum concn. which decreased as the chain length of the alcohol increased. At higher concns. inactivation occurred. The activation was practically instantaneous and reversible, the inactivation slower and irreversible. No activation of the hydrolysis of the acetylcholine by the serum enzyme was observed, only a competitive reversible inhibition over the same alcohol concn. range. The hypothesis that the activation was primarily an interference with the inhibition by excess substrate, was examined by studying the effect of substrate concn. In the hydrolysis of acetyl-beta-methylcholine by brain enzyme, the activation observed at high substrate concentrations changed at low substrate concns. to an inhibition. Specific surface-active agents did not cause activation of the enzyme. The importance of the substrate concn. in the study of cholinesterase activity was underlined by this work.

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