THE INTERACTION OF RABBIT MUSCLE ALDOLASE WITH NADH

被引：3
作者：
CHUMACHENKO, YV
SYTNIK, AI
DEMCHENKO, AP
机构：
[1] A.V. Palladin Institute of Biochemistry, Academy of Sciences of the Ukrainian SSR, Kiev
来源：
BIOCHIMICA ET BIOPHYSICA ACTA | 1990年 / 1038卷 / 02期
关键词：
(Rabbit muscle); Aldolase; Fluorescence; NAD binding domain;
D O I：
10.1016/0167-4838(90)90216-3
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Fluorescence studies on both the emission of aldolase and NADH bound to the enzyme were carried out. Aldolase was found to bind four molecules of NADH with KD = 6.0 ± 0.3 μM. KD values for NADPH and NAD+ were 41 ± 4 μM and 140 ± 30 μM, respectively. The affinity to NADH was comparable with that of some NAD-dependent dehydrogenases, and was not affected by the substrate or the inhibitor. © 1990.
引用
收藏
页码：274 / 276
页数：3
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