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

  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},
  volume={30 14},
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.
Abstract Rat liver cytosol was shown previously by us to contain multiple forms of 3α-hydroxysteroid dehydrogenase. Two (F 4 -II and -III) of the seven forms were purified to homogeneity, and four (FExpand
Carbonyl reductase of dog liver: purification, properties, and kinetic mechanism.
Steady-state kinetic measurements in both directions suggest that the reaction proceeds through a di-iso ordered bi-bi mechanism. Expand
Purification and properties of a metyrapone-reducing enzyme from mouse liver microsomes--this ketone is reduced by an aldehyde reductase.
It is concluded that the microsomal metyrapone-reducing enzyme belongs to the family of carbonyl reductases, but differs from the common patterns of their classification with regard to cofactor requirement and inhibitor susceptibility. Expand
Isolation and characterization of multiforms of aldehyde reductase in chicken kidney.
Three multiforms of NADPH-dependent aldehyde reductase have been purified to homogeneity from chicken kidney and it was demonstrated using antibodies against one of the high-Km forms and the low-KM form of aldehydes that the two high- Km forms were immunologically identical with each other but not with the low -Km form. Expand
The metabolite ratio as a function of chloral hydrate dose and intracellular redox state in the perfused rat liver.
The TCE/TCA ratio was altered according to the concentration of CH, and to the redox level of pyridine nucleotides in the liver, to study which reaction is predominant at the physiological redoxlevel in intact liver cells. Expand
Comparative study of the tissue distribution of NADH and NADPH-dependent chloral hydrate reducing enzymes in the rat
NADH and NADPH-dependent CH-reducing activities were investigated in various organs of the rat in order to investigate comparative studies of the tissue distribution of CH- reducing enzymes. Expand
Aldehyde dismutation catalyzed by pulmonary carbonyl reductase: kinetic studies of chloral hydrate metabolism to trichloroacetic acid and trichloroethanol.
The kinetics of the NAD(P)(+)-linked aldehyde dismutation by pulmonary carbonyl reductase of guinea pig were studied and it is suggested that lysine residues are essential for catalysis. Expand
Reduction of 3-keto-5β-cholanoic acid to lithocholic and isolithocholic acids by human liver cytosol in vitro
Abstract The formation of lithocholic and isolithocholic acids from 3-keto-5β-cholanoic acid by human liver cytosol was examined in vitro. Liver cytosol was incubated at various pH levels withExpand
NAD+-dependent ethanol oxidation: Redox effects and rate limitation
  • T. Cronholm
  • Medicine, Chemistry
  • Pharmacology Biochemistry and Behavior
  • 1983
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


Purification and properties of NADPH-dependent aldehyde reductase from human liver.
Results from polyacrylamide gel electrophoresis with and without sodium dodecyl sulfate, gel filtration, and ultracentrifugation suggest a monomeric structure of aldehyde reductase, similar to other monomersic and oligomeric dehydrogenases. Expand
Rat liver daunorubicin reductase. An aldo-keto reductase.
This reactivity with d-glucuronolactone suggests a normal role of daunorubicin reductase in ascorbic acid synthesis or in the glucuronic acid cycle, or both. Expand
Purification and properties of reductases for aromatic aldehydes and ketones from guinea pig liver.
NADPH-dependent enzymatic reduction of aromatic aldehydes and ketones observed in the cytosol of guinea pig liver was mediated by at least three distinct reductases (AR 1, AR 2, and AR 3), which wereExpand
The presence of two NADPH-linked aromatic aldehyde-ketone reductases different from aldehyde reductase in rabbit liver.
Abstract Three NADPH-linked aldehyde reductases (F 1 , F 2 and F 3 ) could be separated by DEAE-cellulose chromatography from rabbit liver cytosol. These enzymes could be distinguished in regard toExpand
Heterogeneity of alcohol dehydrogenase enzymes in various tissues
Abstract The total aldehyde reducing capacity of various tissues, including liver, lung, brain, heart and testes, was determined with propionaldehyde or m -nitrobenzaldehyde as substrate. With eachExpand
Resolution and partial characterization of two aldehyde reductases of mammalian liver.
Investigation of NADP-dependent aldehyde reductase activity in mouse liver led to the finding that two distinct reductases are separable by DE52 ion exchange chromatography, indicating that it is the aldyhyde reductionase recently reported to be identical to NADp-L-gulonate dehydrogenase. Expand
Metabolism of trichloroethylene.
The general features of trichloroethylene metabolism in vitro were demonstrated by the conversion of trICHloroethyleme to the three metabolites by the 700 g supernatant fraction of rat liver in 2 hr. Expand
Rat liver aldehyde reductase.
Abstract Rat liver aldehyde reductase is a soluble constitutive enzyme having the ability to catalyze the reduction of several natural aldehydes such as lactaldehyde, glyceraldehyde,Expand
Aldehyde reductase from rat liver is a 3α-hydroxysteroid dehydrogenase
Abstract Rat liver was previously shown to contain [V.G. Erwin and R.A. Deitrich, Biochem. Pharmacol. 21 , 2915 (1972)] two aldehyde reductases (EC in addition to alcohol dehydrogenase (ECExpand
The role of alcohol dehydrogenase in the metabolism of chloral hydrate.
  • P. Friedman, J. Cooper
  • Chemistry, Medicine
  • The Journal of pharmacology and experimental therapeutics
  • 1960
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