CHOLINE ESTERASE AND THE THEORY OF CHEMICAL MEDIATION OF NERVE IMPULSES

Abstract

The maximum choline esterase activity of the superior cervical ganglion of the cat was measured and found to be, on the average, equivalent to the splitting of 0.10γ of acetyl choline chloride per second per milligram of fresh tissue at a pH of 7.4 and 38°. The least possible time required for destruction of the ester liberated by one nerve impulse was calculated to be 0.015σ. The dissociation constant of the reaction between the enzyme and acetyl choline chloride was determined, and a value of 0.001 was obtained. From the value of the dissociation constant, the time for hydrolysis at the minimum rate was calculated to be about 8 seconds. It was shown that a localization of enzyme and substrate within the ganglion cell would have to exist in order that enzymatic destruction of acetyl choline liberated by nerve impulses occur within the span of the refractory period.