Hydrolysis of ester-type drugs by the purified esterase from human intestinal mucosa

Jpn J Pharmacol. 1979 Feb;29(1):17-25. doi: 10.1254/jjp.29.17.


Esterase from human intestinal mucosa was purified 210 fold by solubilization 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 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.

MeSH terms

  • Aspirin / metabolism
  • Carbenicillin / metabolism
  • Carboxylic Ester Hydrolases / antagonists & inhibitors
  • Carboxylic Ester Hydrolases / isolation & purification
  • Carboxylic Ester Hydrolases / metabolism
  • Esterases / isolation & purification
  • Esterases / metabolism*
  • Esters
  • Humans
  • Hydrolysis
  • Intestinal Mucosa / enzymology*
  • Phosphates / pharmacology
  • Substrate Specificity


  • Esters
  • Phosphates
  • Esterases
  • Carboxylic Ester Hydrolases
  • Carbenicillin
  • Aspirin