Abstract
An NADPH‐linked aldehyde reductase has been purified some 600‐fold from the supernatant fraction of a pig brain homogenate. Subcellular distribution studies show that the enzyme is almost exclusively located in the cytosol. The enzyme has a molecular weight of 29000 and an isoelectric point of 5.8. The enzyme reduces a wide range of aliphatic and aromatic aldehydes, including some biogenic aldehydes. Ketones are not reduced. Specificity studies carried out on the enzyme suggest that substituted phenylglycolaldehydes are reduced far more readily than the corresponding substituted phenylacetaldehydes. Ethanol, reserpine and several aldehyde dehydrogenase and liver alcohol dehydrogenase inhibitors do not affect the activity of brain NADPH‐linked aldehyde reductase. 0.1 mM sodium barbitone markedly inhibits the enzyme.
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