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Molecular Pharmacology, Vol 4, 452-456, Copyright © 1968 by the American Society for Pharmacology and Experimental Therapeutics

The Inhibition of Acetylcholinesterase by 2-Pyridinealdoxime Methyl Halide

L. A. MOUNTER 1 and R. I. ELLIN 1

1 Weapons Development and Evaluation Laboratory, Naval Weapons Laboratory, Dahlgren, Virginia 22448, and Medical Research Laboratory, Edgewood Arsenal, Maryland 21040

The effect of varying concentrations of 2-pyridinealdoxime methyl chloride (2-PAM) on the hydrolysis of acetyl-beta-methylcholine and acetylcholine by electric eel cholinesterase has been studied. With the former substrate the effects are predominantly competitive, but there are noncompetitive contributions. The dissociation constant of the enzyme-inhibitor complex has been evaluated, together with other kinetic constants. The relative magnitudes of these constants determine the kinetic behavior of the enzymic hydrolysis. Inhibition by 2-PAM chloride and other quaternary compounds may be significant in the interpretation of pharmacological and biochemical experiments.

Submitted on July 11, 1967
Revised on June 10, 1968







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