The purification and properties of an alcohol dehydrogenase from mouse liver

Abstract

1. 1. An alcohol dehydrogenase (alcohol: NAD oxidoreductase, EC ( [middle dot] [middle dot] ) was isolated from the supernatant fraction of mouse liver and purified 206-fold.2. 2. A number of aliphatic aldehydes, ranging from acetaldehyde to octadecanal, as well as benzaldehyde and isobutanal, were capable of being reduced by the enzyme. Km values ranged from 9.9 x 10-4 to 2.5 x 10-6 M.3. 3. Cetyl alcohol was slowly oxidized to the aldehyde by the enzyme m the presence of NAD+. However, attempts to oxidize ethanol were unsuccessful.4. 4. The enzyme showed a pH optimum at pH 6.8 with irreversible denaturation occurring below pH 5 and above pH 9.