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  • 1
    ISSN: 1432-0738
    Keywords: Aldehyde dehydrogenase ; Enzyme induction ; Phenobarbital ; 3-Methylcholanthrene ; Genetic control
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The responsiveness of the hepatic supernatant NAD+-dependent aldehyde dehydrogenase with a high Km value (high Km-AldDH) to phenobarbital (PB) and 3-methylcholanthrene (3-MC) treatment was studied in male rats of three strains; Wistar, Long-Evans, and Sprague-Dawley. A remarkable strain difference in the response of the enzyme to PB or 3-MC was observed. In rats of the Wistar strain the enzyme activity remained unchanged (“non-responsive”) in all rats after treatment with PB while it increased (“responsive”) 5- to 19-fold in all rats after treatment with 3-MC. The enzyme activity increased 8- to 20-fold and 2- to 8-fold respectively after treatment with PB and 3-MC in all rats of the Long-Evans strain. In rats of the Sprague-Dawley strain the enzyme activity remained unchanged in half of all the rats treated with PB or 3-MC and increased 2- to 7-fold over the basal level in half of the treated rats. The non-responsive rats to PB were all responsive to 3-MC treatment while the responsive rats to PB were responsive in 65% and non-responsive in 35% to 3-MC treatment.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-0738
    Keywords: Trichloroethylene ; Ethanol metabolism ; Acetaldehyde ; Aldehyde dehydrogenases
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The liver NAD+-dependent aldehyde dehydrogenase (AldDH) activity and the acetaldehyde level in the blood during ethanol metabolism after trichloroethylene (trichlene) exposure were studied in rats. Trichlene inhalation caused large elevations in acetaldehyde levels during ethanol metabolism and caused decreases in the activity of the AldDH with a low Km value in mitochondrial and soluble fractions of liver cells. No significant effects were found in the activity of the high Km-enzyme in mitochondrial, soluble and microsomal fractions. Time course of inhibition of the mitochondrial low Km-enzyme and that of elevations in acetaldehyde levels during ethanol metabolism after trichlene exposure were similar. These findings suggest that acetaldehyde formed from ethanol in vivo is oxidized primarily by the mitochondrial low Km-enzyme.
    Type of Medium: Electronic Resource
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