title: Isotope effects in the binding of NADH to equine liver alcohol dehydrogenase.
abstract: The isotope effect upon the binding constant of NADH to equine liver alcohol dehydrogenase is determined with a method in which the isotopic ratio is measured concurrently in the free and the bond form of the coenzyme, by use of a propellent-pressurized ultrafiltration apparatus for separation of the two. The value for KH/KD for the binding constants was 1.00 +/- 0.02 at pH 10.3 and 25 degrees C.
mesh_terms: D000429:Alcohol Oxidoreductases; D000818:Animals; D001665:Binding Sites; D005612:Freeze Drying; D006736:Horses; D007700:Kinetics; D008099:Liver / Q000201:enzymology*; D009243:NAD; D010084:Oxidation-Reduction; D011485:Protein Binding
chemical_list: D009243:NAD; D000429:Alcohol Oxidoreductases