Ethanol oxidation by a component of liver microsomes rich in cytochrome P-450.

@article{Mezey1973EthanolOB,
  title={Ethanol oxidation by a component of liver microsomes rich in cytochrome P-450.},
  author={Esteban Mezey and James John Potter and W. D. C. Reed},
  journal={The Journal of biological chemistry},
  year={1973},
  volume={248 4},
  pages={
          1183-7
        }
}

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References

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Hepatic Microsomal Ethanol Oxidation
TLDR
It is concluded that the NADPH-dependent microsomal ethanol-oxidizing system of Lieber and DeCarli is due to a hydrogen peroxide formation from NADPH and a subsequent peroxidation of ethanol by contaminating catalase.
Studies on the rate of reduction of hepatic microsomal cytochrome P-450 by reduced nicotinamide adenine dinucleotide phosphate: effect of drug substrates.
TLDR
The data suggest that the complexes formed between cytochrome P-450 and type I compounds are more readily reduced by NADPH than is the endogenous hemoprotein.
Hepatic microsomal ethanol-oxidizing system. In vitro characteristics and adaptive properties in vivo.
TLDR
The existence of a microsomal ethanol-oxidizing system, especially its capacity to increase in activity adaptively after ethanol feeding, may explain various effects of ethanol, including proliferation of hepatic smooth endoplasmic reticulum, induction of other hepaticmicrosomal drug-detoxifying enzymes, and the metabolic tolerance to ethanol which develops in alcoholics.
Cytochrome P-450 as a microsomal peroxidase utilizing a lipid peroxide substrate.
Ethanol oxidation by liver microsomes: evidence against a separate and distinct enzyme system.
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