title: Subcellular localization of aldehyde reductase activities in ox brain.
abstract: The distribution of the two principal isoenzymes of aldehyde reductase (EC 1.1.1.2) has been studied in ox brain. The more active of these, which has been termed the high-Km enzyme, has been shown to be located in the cytosol and the less abundant low-Km form has a similar localization. p-Nitrobenzaldehyde, which has been used as a substrate in previous studies, caused the reduction of NADH in the presence of the mitochondrial fraction, but mixed substrate experiments with 1,3-dinitrobenzene and the effects of pH on the activity indicate that this is due to the presence of a nitro reductase activity which has been recently described (Köchli, Wermuth & von Wartburg (1980) Biochim. Biophys. Acta 616, 133-142] rather than to the low-Km aldehyde reductase activity. Fractionation of the mitochondria indicated this activity to be largely confined to the mitochondrial inner membrane.
mesh_terms: D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism; D000818:Animals; D001547:Benzaldehydes / Q000378:metabolism; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D002458:Cell Fractionation; D004072:Digitonin / Q000494:pharmacology; D005969:Glutamate Dehydrogenase / Q000378:metabolism; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D011725:Pyridines / Q000378:metabolism; D013347:Subcellular Fractions / Q000201:enzymology; D013367:Submitochondrial Particles / Q000201:enzymology
chemical_list: D000447:Aldehydes; D001547:Benzaldehydes; D007527:Isoenzymes; D011725:Pyridines; C033525:4-carboxybenzaladehyde; C014785:3-pyridinaldehyde; D000429:Alcohol Oxidoreductases; C019642:alcohol dehydrogenase (NADP+); D005969:Glutamate Dehydrogenase; D004072:Digitonin