Abstract
We have identified a novel reaction in which acetaldehyde promotes rat hepatic cytosolic catalysis of O 2 consumption coupled with glutathione oxidation without apparent release of activated forms of O 2. Acetaldehyde is not consumed in the reaction. The reaction (O 2 consumption or oxidized glutathione production) is saturable with respect to varying glutathione (K′ m⋍20–45 μM ) but not at high acetaldehyde concentrations. However, activity in the range of acetaldehyde found in liver from alcohol metabolism (10–100 μM ) appeared to be saturable (K′ m⋍25–50 μM ). Since neither acetaldehyde-dependent glutathione loss nor O 2 consumption is detectable in guinea pig hepatic cytosol or hepatic cytosol from selenium-deficient rats, we propose that acetaldehyde interacts with glutathione peroxidase, converting the enzyme into a glutathione oxidase.
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 callMore From: Biochemical and Biophysical Research Communications
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.
