NADH与马肝醇脱氢酶结合中的同位素效应。
Isotope effects in the binding of NADH to equine liver alcohol dehydrogenase.
作者信息
deJuan E, Taylor K B
出版信息
Biochemistry. 1976 Jun 15;15(12):2523-7. doi: 10.1021/bi00657a005.
PMID:181045
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.
摘要
利用一种通过推进剂加压超滤装置分离辅酶的游离形式和结合形式并同时测量同位素比率的方法，测定了NADH与马肝醇脱氢酶结合常数的同位素效应。在pH 10.3和25℃条件下，结合常数的KH/KD值为1.00±0.02。
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