Titlebook: Alcohol and Aldehyde Metabolizing Systems-IV; Ronald G. Thurman Book 1980 The Editor(s) (if applicable) and The Author(s), under exclusive

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Data Preprocessing in Data Miningts a substantial preference for 2-hydroxy aldehydes (Turner and Tipton, 1972b; Wermuth and Münch, 1979). Rat brain and other tissues contain at least one other aldehyde reductase (AR2 or “l(fā)ow-K.”) that is similar to or identical with aldose reductase (EC 1.1.1.21) (Turner and Tipton, 1972b). This la

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Role of Hydroxyl Radicals in Microsomal Oxidation of Alcoholsengers was specific since these agents had no effect on catalase-dependent oxidation of ethanol, microsomal drug metabolism or microsomal electron transfer. Chemical evidence for production of ?OH during microsomal electron transfer was provided by the generation of appropriate products from ?OH sca

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On the Possible Relationship of Cytochrome P-450 to Alcohol Metabolism: Fundamental Aspects of the Misozymes, one of which is induced . by the administration of aromatic hydrocarbons, as well as several forms which are less well characterized and not known to be inducible. The various cytochromes exhibit partially selective but overlapping activities with a variety of substrates. Additional compon

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Isozymes of Alcohol Dehydrogenase and Aldehyde Dehydrogenase in Japanese and their Role in Alcohol S enzymes have been proposed to play an important role in sensitivity to alcohol associated with facial flushing and other subjective symptoms (Stamatoyannopoulos et al., 1975; Goedde et al., 1979b; Harada et al., 1979).

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On the Interaction of Human Liver Aldehyde Dehydrogenase E1 Isoenzyme with Disulfiram and Iodoacetames disulfiram/tetrameric E., is immediately inhibited to within 10% of control activity. The inhibition is reversed by 0.1% (v/v) mercaptoethanol, indicating disulfide bridge formation. An indirect attempt to locate, on maps, a peptide binding disulfiram has yielded inconsistent results. Iodoacetami