Related Experiment Video
Updated: Aug 17, 2026

Bioluminescence Imaging of NADPH Oxidase Activity in Different Animal Models
Published on: October 22, 2012
Cytochrome P450 oxidase activity and its role in NADPH dependent lipid peroxidation
Abstract:
A comparison is made between microsomal NADPH-dependent H2O2 production and malondialdehyde (MDA) formation in rat liver microsomes, obtained from phenobarbital pretreated rats. An increase in H2O2 formation was observed during NADPH-dependent disposition (10 min) of 100 microM diazepam (33%) and 2 mM hexobarbital (69%). In contrast orphenadrine (100 microM) and its mono-N-demethylated metabolite tofenacine (100 microM) decreased the H2O2 formation (35% and 55%, respectively). However, all these substrates were found to inhibit NADPH-dependent lipid peroxidation (60 min), estimated by measuring MDA formation, to various extents. These data strongly suggest that the oxidase activity of cytochrome P450 (H2O2 production) is not involved in a rate-limiting step in NADPH-dependent lipid peroxidation.
More Related Videos
07:29Cell-free Biochemical Fluorometric Enzymatic Assay for High-throughput Measurement of Lipid Peroxidation in High Density Lipoprotein
Published on: October 12, 2017
08:57Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Related Concept Videos
Role of Reduced Coenzymes NADH and FADH₂
Peroxisomes
Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox property is crucial in...
Electron Transport Chain: Complex III and IV
Bioactivation and Tissue Toxicity
Redox Reactions