Determination of butyrylcholinesterase inhibition using ion transfer across the interface between two immiscible liquids

Article abstract of DOI:10.1021/ac00073a011

An investigation was made into the inhibition of the enzyme butyrylcholinesterase by paraoxon (diethyl p-nitrophenyl phosphate), using butyrylcholine chloride as the substrate. Experimental measurement was based on the transfer of the butyrylcholine cation across the interface between water and 1,2-dichloroethane using cyclic voltammetry. By this method it was possible to determine the rate constants for both the inhibition of the enzyme and the hydrolysis of butyrylcholine.