Chumachenko Y V, Sytnik A I, Demchenko A P
A.V. Palladin Institute of Biochemistry, Academy of Sciences of the Ukrainian SSR, Kiev.
Biochim Biophys Acta. 1990 Apr 19;1038(2):274-6. doi: 10.1016/0167-4838(90)90216-3.
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.