Abstract
Acetylcholinesterase was partially purified by salt fractionation with ammonium sulphate, anion exchange chromatography on DEAE-Cellulose and gel filtration on Sephadex G-200 column to specific activity of 2U/mg of total protein. 32 fold purification was achieved. Cyclophosphamide, anisomycin and puromycin were studied with respect to their inhibition role on acetylcholinesterase. Cyclophosphamide showed mixed noncompetitive-uncompetitive inhibition, while anisomycin showed competitive and puromycin showed noncompetive inhibition with Ki values 5.6, 1.75 and 0.35 mM respectively.