The effect of phenylacetic acid on cholinesterase activity and on some isoenzymes of esterases and cholinesterases of peain vitro

Phenylacetic acid at 1.5 × 10^-3 M inhibits the activity of some esterase isoenzymes from pea leaves separated by means of polyacrylamide gel electrophoresis. Some of the inhibited esterases show cholinesterase activity. Inhibition of the total activity has been demonstrated with a partially purified protein fraction from pea leaves containing choline esterase. The inhibition constant established after Dixon was 7.9 × 10^-3 M and the type of inhibition was competitive.