HYDROLYSIS OF ESTER-TYPE DRUGS BY THE PURIFIED ESTERASE FROM HUMAN INTESTINAL MUCOSA

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Abstract
Esterase from human intestinal mucosa was purified 210-fold by solubilizaiton with Triton X-100, chromatography on DEAE-cellulose, Sephadex G-100 and hydroxylapatite, and isoelectric focusing. The purified esterase showed a single band by polyacrylamide gel electrophoresis. The MW of the purified esterase was estimated to be about 55,000 by gel filtration on Sephadex G-150 and the isoelectric point was 5.02. The purified esterase was strongly inhibited by diethyl p-nitrophenyl phosphate (E-600) and DFP but was not inhibited by eserine sulfate and p-chloromercuribenzoate. The purified from human intestinal mucosa is apparently one of the carboxylesterases. The purified esterase hydrolyzed ester-type drugs, i.e., aspirin, clofibrate, indanyl carbenicillin and procaine, but did not hydrolyze amide-type drugs and choline-type drugs.