Spectrophotometric Analysis of Human CYP2E1-Catalyzed p -Nitrophenol Hydroxylation
作者： Thomas K. H. Chang , Charles L. Crespi , David J. Waxman
DOI: 10.1385/0-89603-519-0:147
关键词: CYP2E1 、 Nitrophenol 、 Catalysis 、 Trichloroacetic acid 、 Hydroxylation 、 Enzyme 、 Microsome 、 Neutralization 、 Chemistry 、 Chromatography
摘要: The cytochrome P450 enzyme CYP2E1 catalyzes the oxidative metabolism of many solvents and other small organic molecules. A spectrophotometric method is described for determination activity by monitoring formation p-nitrocatechol from p-nitrophenol cDNA-expressed or isolated liver microsomes. enzymatic product, p-nitrocatechol, assayed at 535 nm after acidification reaction mixture with trichloroacetic acid followed neutralization using 2 M NaOH. This applicable to studies P450-catalyzed hydroxylation activity.
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