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- W249968689 abstract "This chapter discusses studies on the site of fluorescamine inhibition of cytochrome p-450-mediated reactions. Cytochrome P-450 and NADPH-cytochrome P-450 reductase from the liver microsomes of phenobarbital-treated rats and cytochrome P-448 from the liver microsomes of 3-methylcholanthrene-treated rats were purified. Chemical modification of the hemeproteins or reductase with fluorescamine was carried out by adding various amounts of fluorescamine in a constant volume of acetone to the appropriate protein in phosphate buffer. Reactions were performed at room temperature and treated samples sat for 10 min to allow excess reagent to hydrolyze. The modified proteins were then tested. It was found that when added to microsomes of phenobarbital-treated rats, fluorescamine markedly inhibited benzphetamine N-demethylation and produced a fluorescent product. Addition of fluorescamine to NADPH–cytochrome P-450 reductase at a mole ratio of up to 100:1 produced a fluorescent derivative but had very little effect on benzphetamine N-demethylation as assayed with the reconstituted system. As the modified reductase is able to reduce cytochrome P-450, there does not appear to be an accessible, essential lysine or N-terminal amino group in the active site of the reductase." @default.
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- W249968689 date "1980-01-01" @default.
- W249968689 modified "2023-09-26" @default.
- W249968689 title "STUDIES ON THE SITE OF FLUORESCAMINE INHIBITION OF CYTOCHROME P-450-MEDIATED REACTIONS" @default.
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- W249968689 doi "https://doi.org/10.1016/b978-0-12-187701-9.50038-3" @default.
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