Abstract
Oxidation of [ 75Se]dimethylselenide by rat liver and lung microsomes and by purified flavin-containing monooxygenase from pig liver was demonstrated. Quantitation of the nonvolatile product showed a 1:1 stoichiometry with NADPH oxidation, consistent with selenoxide formation. The apparent K m for dimethylselenide was 0.7 μM with rat liver microsomes and 0.3 μM with purified pig liver enzyme. Facile reversal of dimethylselenide oxidation by reducing agents present in microsomes, and by glutathione, indicates that redox cycling can occur. Unlabeled dimethylselenoxide carrier circumvented reduction of the labeled product, permitting quantitation. This is the first demonstration of a naturally occurring selenium substrate for the microsomal flavin-containing monooxygenase.
Sign-in/Register to access full text options 
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 callDisclaimer: 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.
