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• W2055225624 abstract "Abstract— The presence of a nonspecific NADH-linked aldehyde reductase was demonstrated in various regions of bovine brain in vitro. With m-nitrobenzaldehyde as substrate, the rate of NADH oxidation was approximately 4 nmol.min-1.(mg of protein)-1 in the cerebellum, pons and medulla; but somewhat lower rates [2–3 nmol.min-1.(mg of protein)-l] were obtained in the other areas of the brain examined. The enzyme was localized primarily in the soluble, supernatant fraction of rat brain homogenates. The enzyme from the supernatant fluid fraction of bovine brain was purified approximately 350-fold by ammonium sulphate fractionation and chromatography on calcium phosphate-gel, DEAE-cellulose and Sephadex G200 columns. The partially purified enzyme catalysed the reduction of a number of aldehydes, including substituted benzaldehydes and aliphatic aldehydes of intermediate chain lengths. Short chain aliphatic aldehydes, such as acetaldehyde, were not reduced by the enzyme and butyraldehyde was a poor substrate. With m-nitrobenzaldehyde as substrate, NADH was oxidized at an approximately 10-fold faster rate than NADPH. The pH optimum for the enzyme was 6.75 for aldehyde reduction, whereas the rate of oxidation of m-nitrobenzylalcohol was optimal at pH 10.0 with NAD as the co-substrate. Km and K3 values ranged from 10 μM to 10 mM for various aldehydes and from 10 to 30 μM for the cofactors. Oxidation of NADH by the partially purified enzyme was not inhibited by 10m pyrazole or by 1 mM phenobarbital. However, the enzyme activity was inhibited by approximately 60 percent by 1 mM chlorpromazine or by 5 mM 1,10-orthophenanthroline. Our data demonstrate that the enzyme is not only separable from the NADPH-linked aldehyde reductase described previously by TABAKOFF and ERWIN, but also is quite different in substrate specificity and inhibitor sensitivity from the ‘classical’, pyrazole-sensitive, NAD- linked alcohol dehydrogenase (EC 1.1.1.1)." @default.
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• W2055225624 date "1972-10-01" @default.
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• W2055225624 title "PURIFICATION AND CHARACTERIZATION OF AN NADH-LINKED ALDEHYDE REDUCTASE FROM BOVINE BRAIN" @default.
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• W2055225624 doi "https://doi.org/10.1111/j.1471-4159.1972.tb01280.x" @default.
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