Abstract
The effect of varying concentrations of 2-pyridinealdoxime methyl chloride (2-PAM) on the hydrolysis of acetyl-β-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.
- Copyright ©, 1968, by Academic Press Inc.
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