Identification of aspirinase with one of the carboxylesterases requiring a thiol group.
Aspirin-hydrolysing activity in guinea-pig liver is located mainly in the microsomal fraction. This activity was found by electrophoresis to be due to a single carboxylesterase band, out of 12 bands revealed with alpha-naphthyl acetate as substrate. The activity is inhibited completely and irreversibly by the carboxylesterase inhibitor bis-(-4-nitrophenyl) hydrogen phosphate, and also by thiol-blocking reagents.
D000818:Animals; D002265:Carboxylic Ester Hydrolases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006168:Guinea Pigs; D008099:Liver / Q000201:enzymology*; D013347:Subcellular Fractions / Q000201:enzymology; D013439:Sulfhydryl Reagents / Q000494:pharmacology
D013439:Sulfhydryl Reagents; D002265:Carboxylic Ester Hydrolases; C018737:acetylsalicylic acid hydrolase