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:
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