Evidence for site equivalence in the reaction mechanism of horse liver alcohol dehydrogenase with aromatic substrates at alkaline pH

Biochemistry ◽  
1977 ◽  
Vol 16 (13) ◽  
pp. 2916-2922 ◽  
Author(s):  
Charles F. Weidig ◽  
Herbert R. Halvorson ◽  
Joseph D. Shore
Keyword(s):  
Reaction Mechanism ◽  
Alcohol Dehydrogenase ◽  
Alkaline Ph ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Aromatic Substrates ◽  
Horse Liver

Purification of Isoenzyme and Coenzymes for Kinetic Study of Horse Liver Alcohol Dehydrogenase

1972 ◽  
Vol 50 (12) ◽  
pp. 1376-1384 ◽  
Author(s):  
Patricia A. Gurr ◽  
Patricia M. Bronskill ◽  
Charles S. Hanes ◽  
J. Tze-Fei Wong
Keyword(s):  
Reaction Mechanism ◽  
Alcohol Dehydrogenase ◽  
Kinetic Study ◽  
Kinetic Studies ◽  
Horse Liver Alcohol Dehydrogenase ◽  
Liver Alcohol Dehydrogenase ◽  
Electrophoretic Mobilities ◽  
Horse Liver ◽  
Starch Gel ◽  
Specific Activities

The isoenzymic forms of the alcohol dehydrogenase (EC 1.1.1.1) of horse liver have been separated by chromatography on carboxymethylcellulose column and identified in terms of their electrophoretic mobilities in the starch gel. Purified isoenzyme fraction C1, which was highest in both total and specific activities, was stable toward rechromatography on carboxymethylcellulose, electrophoresis in starch gel, as well as storage in solution. It therefore satisfied the requirements for use in kinetic studies on the reaction mechanism of the enzyme. Toward the same end, procedures are also described for preparing purified NAD+ and NADH in solution forms which were stable in storage for several days.

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