[Studies on phagocytosis of bacteria and latex particles by leukemic cells in childhood acute leukemia (author's transl)].
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Biomedical subjects
Publications and source records attributed to M Tsukada.
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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.
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The effect of phenobarbital on activities of aldehyde dehydrogenases in the subcellular fractions was studied in vivo in rats of three strains. Regarding the responses of the mitochondrial and microsomal enzymes to phenobarbital treatment no difference among the strains was observed. Regarding the responses of the supernatant enzyme remarkable strain differences were observed. In rats of the Long-Evans strain the high Km-enzyme activity increased as much as 15-fold above control levels by phenobarbital treatment. By contrast, in rats of the Wistar strain the high Km-enzyme activity was unchanged in all rats by treatment with phenobarbital. In rats of the Sprague-Dawley strain the high Km-enzyme activity remained unchanged in 52% of all rats treated with phenobarbital and was increased approximately 4-fold over control levels in 48% of treated rats.
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