Isotope effects in the binding of NADH to equine liver alcohol dehydrogenase
- 15 June 1976
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 15 (12), 2523-2527
- https://doi.org/10.1021/bi00657a005
Abstract
The isotope effect upon the binding constant of NADH to equine liver alcohol dehydrogenase [EC 1.1.1.1] is determined with a method in which the isotopic ratio is measured concurrently in the free and the bound form of the coenzyme, using a propellent-pressurized ultrafiltration apparatus for separation of the two. The value for KH/KD [binding constant for Proton/binding constant for deuteron] was 1.00 .+-. 0.02 at pH 10.3 and 25.degree. C.This publication has 4 references indexed in Scilit:
- Evidence for an acid-catalyzed αβ epimerization in pyridine nucleotidesBiochemistry, 1968
- Equilibrium Reaction Rates and the Mechanisms of Bovine Heart and Rabbit Muscle Lactate DehydrogenasesJournal of Biological Chemistry, 1964
- Isotope and solvent effects of deuterium on rabbit-muscle lactate dehydrogenaseBiochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects, 1964
- Studies on the Mechanism of Enzyme-Catalyzed Oxidation Reduction Reactions. IV. A Proposed Mechanism for the Over-all Reaction Catalyzed by Liver Alcohol Dehydrogenase*Biochemistry, 1962