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• W286403011 abstract "ABSTRACT The metabolism of hexobarbital enantiomers by 9000g liver supernatant was determined in mice and rats. Both male and female mice and rats metabolize hexobarbital stereospecifically. In mice the 1-enantiomer is metabolized faster, whereas the opposite was observed in rats. The kinetics of metabolism and type I binding to cytochrome P-450 of the enantiomers was compared in female mice and male rats. In mice K m equaled K S for type I binding, but in rats K m exceeded K S . This suggests that in mice the type I binding site is the active site of the enzyme, whereas in rats this cannot be proved. In female rats the A max for type I binding of the enantiomers differs, indicating a binding to different cytochrome P-450 subspecies. Comparison of the enhancement of NADPH-cyt. P-450 reductase activity by the enantiomers with their rate of metabolism at the same concentration revealed that in rats the reduction of the cytochrome P-450-substrate complex cannot be rate-limiting for the total reaction, whereas in mice this cannot be disproved. This would explain the apparent discrepancy between the kinetics of type I binding and metabolism in rats, which was not found in mice." @default.
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• W286403011 date "1977-01-01" @default.
• W286403011 modified "2023-10-07" @default.
• W286403011 title "METABOLISM OF HEXOBARBITAL ENANTIOMERS AND INTERACTION WITH CYTOCHROME P-450 IN MALE AND FEMALE MICE AND RATS" @default.
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• W286403011 doi "https://doi.org/10.1016/b978-0-08-021523-5.50075-4" @default.
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