Abstract

Hepatic drug metabolizing enzymes were significantly decreased in Ehrlich ascites tumour-bearing mice. A protein inhibitor of hepatic drug metabolizing enzymes was isolated from Ehrlich ascites cells and purified. This involved ammonium sulphate fractionation (60-80%), DEAE, phosphocellulose, Sephadex G-100 and hydroxyapatite column chromatography. Purification attained was 800-fold. The inhibitory protein was effective in decreasing all the components of hepatic mixed-function-oxidase system and drug metabolizing enzymes both in vivo and in vitro. This novel inhibitor may have potential applications in chemical carcinogenesis.

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

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.