Immunochemical study on the participation of cytochrome b5 in drug oxidation reactions of mouse liver microsomes. |
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Authors: | M Noshiro N Harada T Omura |
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Institution: | Department of Biology, Faculty of Science, Kyushu University, Higashi-ku, Fukuoka 812, Japan |
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Abstract: | Highly purified divalent and monovalent antibodies against cytochrome , anti- immunoglobulin G (IG) and anti- Fab', were used in elucidating the role of this cytochrome in the drug-oxidizing enzyme system of mouse liver microsomes. Anti- IG strongly inhibited not only NADH-supported but also NADPH-supported oxidation of 7-ethoxycoumarin and benzo(a)pyrene, but had no inhibitory action on the oxidation of aniline. Anti- Fab' also inhibited NADH-supported and NADPH-supported benzo(a)pyrene hydroxylation. These observations indicate an essential role of cytochrome in the transfer of electrons not only from NADH but also from NADPH to cytochrome P-450 in the microsomal oxidation of some drugs, but not of aniline. |
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