Oxidation of acetaldehyde and presence of aldehyde dehydrogenase in rat erythrocytes.

Rat liver erythrocytes were found to oxidize acetaldehyde at 7 nmoles/min/ml blood at 37 degrees C. This is less than 1% the rate that occurs in liver. An aldehyde dehydrogenase was isolated from erythrocytes, but was not purified. The enzyme had a Km of 170 microM toward acetaldehyde at pH 7.4. The enzyme, which could oxidize both aliphatic and aromatic aldehydes, was more active at pH 9 than at 7. Disulfiram proved to be both an in vivo and in vitro inhibitor of the enzyme. Due to the low total capacity of the erythrocytes to metabolize acetaldehyde, it is doubtful they perform any important role in ethanol metabolism.