Dealkylation studies on inhibited acetylcholinesterase

Abstract
A rapid method for measuring the rate of dealkylation of organophosporus-inhibited enzymes is described. The dealkylation rates have been measured for acetylcholinesterase inhibited by iso-propyl, sec.-butyl, 1,2-dimethylpropyl,1,2,2-trimethylpropyl and cyclohexyl methylphosphonofluoridate, and by diisopropyl phosphoro-fluoridate; they are 1st-order under the conditions used.