Abstract
A chemiluminescence method for determining acetylcholinesterase [AChE] activity is described. AChE activity is measured by monitoring the increase in light emission produced by the accumulation of choline or by determining the amount of choline generated after a short interval. The assay is rapid and sensitive, and uses the natural substrate of the enzyme. Kinetic data obtained with this procedure for AChE from Torpedo marmorata and Electrophorus electricus electric organs were comparable with those obtained previously. It was shown that sodium deoxycholate totally inactivated Torpedo AChE but not the Electrophorus enzyme. Competitive inhibitors of AChE protected the enzyme from inactivation.