Studies on NADPH-dependent chloral hydrate reducing enzymes in rat liver cytosol.

@article{Ikeda1981StudiesON,
  title={Studies on NADPH-dependent chloral hydrate reducing enzymes in rat liver cytosol.},
  author={M. Ikeda and M. Ezaki and S. Kokeguchi and S. Ohmori},
  journal={Biochemical pharmacology},
  year={1981},
  volume={30 14},
  pages={
          1931-9
        }
}
Abstract Chloral hydrate, a sedative hypnotic and also a major metabolite of trichloroethylene in higher animals, is reduced to trichloroethanol by liver extracts. The reducing activity in rat liver cytosol could be separated into four fractions [one NADH- (F 1 ) and three NADPH-dependent (F 2 , F 3 and F 4 )] by DEAE-cellulose column chromatography. By several procedures, F 2 was purified over 1000-fold and F 4 was purified over 600-fold from liver cytosol. As judged from polyacrylamide gel… Expand
Properties of NADPH-dependent carbonyl reductases in rat liver cytosol.
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NAD+-dependent ethanol oxidation: Redox effects and rate limitation
  • T. Cronholm
  • Medicine, Chemistry
  • Pharmacology Biochemistry and Behavior
  • 1983
TLDR
The results indicate that the coenzyme bound to alcohol dehydrogenase is not equilibrated with free coen enzyme, and the dissociation of NADH might be rate-limiting for ethanol oxidation. Expand
Identification of 7α,12α-dihydroxy-5β-cholestan-3-one 3α-reductase as 3α-hydroxysteroid dehydrogenase
A reductase catalyzing the reduction of the 3-ketone group of 7 alpha,12 alpha-dihydroxy-5 beta-cholestan-3-one and 7 alpha-hydroxy-5 beta-cholestan-3-one, which are the intermediates in theExpand
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TLDR
Evidence is offered that the principal mediator of the reduction of chloral hydrate to trichloroethanol in the body is alcohol dehydrogenase, which is shown to be DPNH-dependent. Expand
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