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

被引:35
作者
INOUE, M [1 ]
MORIKAWA, M [1 ]
YAMADA, T [1 ]
SUGIURA, M [1 ]
TSUBOI, M [1 ]
机构
[1] GIFU COLL PHARM,DEPT PHARM,GIFU,GIFU 502,JAPAN
关键词
D O I
10.1254/jjp.29.17
中图分类号
R9 [药学];
学科分类号
1007 ;
摘要
Esterase from human intestinal mucosa was purified 210 fold by solubilization with Triton X-100, chromatography on DEAF-cellulose, Sephadex G-100 and hydroxy lapatite, and isoelectric focusing. The purified esterase showed a single band by polyacrylamide gel electrophoresis. The molecular weight 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 diisopropyl fluorophosphate (DFP), and was not inhibited by eserine sulfate and p-chloromercuribenzoate. The purified esterase from human intestinal mucosa was found to be 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. © 1979, The Japanese Pharmacological Society. All rights reserved.
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页码:17 / 25
页数:9
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