Steady-state study of horse-liver ADH: detection of two kinetically heterogeneous components.
New theoretical considerations and a new approximation strategy were applied to the kinetic analysis of the experimental relationship between the reaction velocity in the steady state and the concentrations of ethanol and NAD. It could be shown that horse-liver ADH consists of two kinetically heterogeneous components.
D000429:Alcohol Oxidoreductases / Q000378:metabolism*; D000818:Animals; D002384:Catalysis; D000431:Ethanol / Q000378:metabolism; D006736:Horses; D007527:Isoenzymes / Q000378:metabolism*; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D009243:NAD / Q000378:metabolism
D007527:Isoenzymes; D009243:NAD; D000431:Ethanol; D000429:Alcohol Oxidoreductases