Abstract
It has been shown with reference to liver microsomes prepared in the presence and in the absence of alpha-tocopherol that structural alterations that may arise from the isolation procedure may affect interplay of carriers in NADP.H oxidation. Study of these alterations is of importance for understanding the influence of different factors of NADP.H oxidase on the involvement of NAD.H in benz(a)pyrene hydroxylation. If the electron transport via NADP.H-dependent flavoprotein is limited, the intense hydroxylation of benz(a)pyrene can be supported by means of chains involved in NAD.H oxidation. Studies have been focused on utilization of NAD.H in benz(a)pyrene hydroxylation and lipid peroxidation.
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.
