Pd. Beattie et al., DETERMINATION OF BUTYRYLCHOLINESTERASE INHIBITION USING ION TRANSFER ACROSS THE INTERFACE BETWEEN 2 IMMISCIBLE LIQUIDS, Analytical chemistry, 66(1), 1994, pp. 52-57
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.