AI Article Synopsis
- NADPH-cytochrome c reductase in Hepa-1 cells increased by 2 times when treated with phenobarbital, but not affected by benz[a]anthracene or TCDD.
- The enzyme has a Km value of 0.57 microM for NADPH, shows inhibition by NADP, and is mostly located in the microsomal fraction.
- Comparison with 3T3 cells indicates that their lower cytochrome c reductase activity correlates with reduced binding of cytochrome P-450 reductase antibody, suggesting its role in the observed activity.
Article Abstract
NADPH-cytochrome c reductase in Hepa-1 cells was induced 2-fold by phenobarbital, but was not induced by benz[a]anthracene or 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD). The apparent Km of the enzyme for NADPH was 0.57 microM; the activity was inhibitable by NADP; and segregated primarily to the microsomal fraction. Cytoplasm of Hepa-1 cells bound antibody to rabbit cytochrome P-450 reductase. 3T3 cells, which possessed one sixth of the cytochrome c reductase activity of Hepa-1 cells, bound correspondingly less cytochrome P-450 reductase antibody. This supports the notion that cytochrome P-450 reductase was responsible for the cytochrome c reductase activity that was measured.
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| http://dx.doi.org/10.1016/0304-3835(83)90231-8 | DOI Listing |
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