Abstract
The in vitro deacylation of N-arylformamides and N-arylacetamides to arylamines was examined in rat liver preparations. When 2-acetylaminofluorene or 2-formylaminofluorene was incubated with rat liver microsomes or cytosol, the deacylated metabolite, 2-aminofluorene, was formed. The deacylating activity of liver microsomes was inhibited by bis(4-nitrophenyl)phosphate and phenylmethanesulfonyl fluoride, inhibitors of carboxylesterase. In contrast, the activity of liver cytosol was inhibited by diisopropyl fluorophosphate, an inhibitor of formamidase. Deacylation of these compounds appear to be mainly catalyzed by carboxylesterase in liver microsomes and formamidase in liver cytosol. 2-Formylaminofluorene, 2-acetylaminofluorene, 1-formylaminopyrene, 4-formylaminobiphenyl, 2-formylaminonaphthalene, 1-formylaminonaphthalene, and 2-acetylaminofluorene were deacylated by formamidase purified from rat liver cytosol. Formamidase catalyzed both N-formylation of arylamines, and deacylation of N-arylformamides and N-arylacetamides.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: Drug metabolism and disposition: the biological fate of chemicals
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.