The interaction of rabbit muscle aldolase with NADH.
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 microM. KD values for NADPH and NAD+ were 41 +/- 4 microM and 140 +/- 30 microM, respectively. The affinity to NADH was comparable with that of some NAD-dependent dehydrogenases, and was not affected by the substrate or the inhibitor.
Chumachenko
Y V
YV
A.V. Palladin Institute of Biochemistry, Academy of Sciences of the Ukrainian SSR, Kiev.
Sytnik
A I
AI
Demchenko
A P
AP
D000818:Animals; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D007700:Kinetics; D009132:Muscles / Q000201:enzymology*; D009243:NAD / Q000378:metabolism*; D011485:Protein Binding; D011817:Rabbits; D013050:Spectrometry, Fluorescence; D013379:Substrate Specificity
D009243:NAD; D005634:Fructose-Bisphosphate Aldolase