title: The interaction of rabbit muscle aldolase with NADH.
abstract: 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.
authors.affiliation: A.V. Palladin Institute of Biochemistry, Academy of Sciences of the Ukrainian SSR, Kiev.
authors.forename: Y V
authors.initials: YV
authors.lastname: Chumachenko
authors.forename: A I
authors.initials: AI
authors.lastname: Sytnik
authors.forename: A P
authors.initials: AP
authors.lastname: Demchenko
mesh_terms: 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
chemical_list: D009243:NAD; D005634:Fructose-Bisphosphate Aldolase