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Antibodies to NADPH-cytochrome P-450 reductase have been used to essentially abolish the contribution of cytochrome P-450 to xenobiotic metabolism by mammalian microsomes. This permits the determination of the activity of the FAD-containing mono-oxygenase and the stoichiometry between substrate, O2 and NADPH, in the microsomal membrane, and in the absence of cytochrome P-450-dependent activity. FAD-containing mono-oxygenase oxidation rates were determined for sulphur- and nitrogen-containing substrates, including: thiols; sulphides; thioamides; primary, secondary and tertiary amines; hydrazines. Although the enzyme in mouse, rabbit, rat and pig microsomes displays similar substrate specificity, some catalytic characteristics are different between species and tissues.
R E Tynes, and
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January 1973,
Drug metabolism and disposition: the biological fate of chemicals,
R E Tynes, and
E Hodgson
May 1973,
The Journal of pharmacology and experimental therapeutics,
R E Tynes, and
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October 1987,
Xenobiotica; the fate of foreign compounds in biological systems,
R E Tynes, and
E Hodgson
January 1988,
Xenobiotica; the fate of foreign compounds in biological systems,
R E Tynes, and
E Hodgson
January 1980,
Pharmacology & therapeutics,
R E Tynes, and
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January 1973,
Drug metabolism and disposition: the biological fate of chemicals,
R E Tynes, and
E Hodgson
January 1990,
Methods in enzymology,
R E Tynes, and
E Hodgson
November 1984,
Xenobiotica; the fate of foreign compounds in biological systems,
R E Tynes, and
E Hodgson
May 1984,
Xenobiotica; the fate of foreign compounds in biological systems,
R E Tynes, and
E Hodgson
May 1994,
Carcinogenesis,
