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The purification and properties of an alcohol dehydrogenase from mouse liver
Kessler, Ralph J.; Ferrell, William J.
Kessler, Ralph J.; Ferrell, William J.
1974-04
Citation:Kessler, Ralph J., Ferrell, William J. (1974/04)."The purification and properties of an alcohol dehydrogenase from mouse liver." International Journal of Biochemistry 5(4): 365-369. <http://hdl.handle.net/2027.42/22383>
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.