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- W265864562 abstract "The redox states of NADPH and NADH systems and of cytochrome P-450 have been studied in rat liver using hemoglobin-free perfusion and isolated hepatocytes from phenobarbital-pretreated rats. The results indicate that in the intact cell control of electron flow through the monooxygenase electron transport chain of the endoplasmic reticulum is exerted by properties intrinsic to the system. Thermodynamically, a plausible description is afforded by a positive increase of the midpoint potential of cytochrome P-450 upon interaction with its substrate, thus facilitating electron flow. In accordance with this, in the intact cell the steady state degree of reduction of cytochrome P-450 is substantially higher in the presence of monooxygenase substrate (30–50 %) than in its absence (about 6 %). The marked decrease in the NADPH/NADP+ ratio of total tissue levels from 4.0 to 2.3 upon addition of monooxygenase substrate is accompanied by a similar decrease in the isocitrate dehydrogenase indicator couple, isocitrate/2-oxoglutarate. Also, the citrate levels decrease significantly due to equilibration by aconitate hydratase. In hepatocytes subfractionated with the digitonin method into cytosolic and mitochondrial fractions, it is shown that not only in the cytosol but also in the mitochondrial compartment there is a decrease of isocitrate and citrate and an increase of 2-oxoglutarate levels upon addition of monooxygenase substrate, e.g. aminopyrine. The cytosolic citrate concentration decreases from 0.17 mM to 0.10 mM during aminopyrine demethylation. This probably explains the inhibition of lipogenesis reported in the literature. Furthermore, in livers from fasted rats, the process of ureogenesis from ammonia, requiring mitochondrial NADPH for amination of 2-oxoglutarate, is partially inhibited; this further illustrates mitochondrial-cytosolic interrelationships occurring during monooxygenation reactions." @default.
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- W265864562 date "1977-01-01" @default.
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- W265864562 title "NICOTINAMIDE NUCLEOTIDE SYSTEMS AND DRUG OXIDATION IN THE LIVER CELL" @default.
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- W265864562 doi "https://doi.org/10.1016/b978-0-08-021523-5.50045-6" @default.
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