DETERMINATION OF BUTYRYLCHOLINESTERASE INHIBITION USING ION TRANSFER ACROSS THE INTERFACE BETWEEN 2 IMMISCIBLE LIQUIDS

An investigation was made into the inhibition of the enzyme butyrylcho linesterase by paraoxon (diethyl p-nitrophenyl phosphate), using butyr ylcholine chloride as the substrate. Experimental measurement was base d on the transfer of the butyrylcholine cation across the interface be tween water and 1,2-dichloroethane using cyclic voltammetry. By this m ethod it was possible to determine the rate constants for both the inh ibition of the enzyme and the hydrolysis of butyrylcholine.