The identity of the serotonin-sensitive aryl acylamidase with acetylcholinesterase from human erythrocytes, sheep basal ganglia and electric eel.

The identity of the serotonin-sensitive aryl acylamidase with acetylcholinesterase from three diverse sources, namely sheep basal ganglia, human erythrocyte membrane and electric eel, was examined. Both the enzymes co-purified with constant ratios of specific activity from all the three sources by different affinity chromatographic techniques. The ratio of acetylcholinesterase to aryl acylamidase activity was highest for basal ganglia, less for erythrocyte and lowest for eel enzymes. Both the purified enzymes co-migrated on polyacrylamide gel electrophoresis either as a single species or multiple species under different conditions. Gel density gradient electrophoresis indicated identical migration rates of both the enzymes. Extraction of the enzymes from the three sources by different techniques of membrane disruption and subsequent gel filtration on Sepharose 6B showed multiple peaks of enzyme activity. Both the enzymes had identical elution profiles on Sepharose 6B gel filtration. All the enzyme peaks from Sepharose 6B on gel electrophoresis showed co-migration of the enzyme activities. Apart from inhibition by serotonin and acetylcholine the purified aryl acylamidases from all the three sources were potently inhibited by neostygmine, eserine and BW 284C51, all strong inhibitors of acetylcholinesterase. It is suggested that the serotonin-sensitive aryl acylamidase is identical with acetylcholinesterase.