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The interaction of NADH with s-malate dehydrogenase isolated from beef heart was studied in 20 mM potassium phosphate (pH 6.9)-1 mM EDTA, with forced dialysis, fluorescence, and temperature-jump techniques. Measurements of the change in fluorescence of NADH when it is titrated with enzyme indicate NADH bound to monomeric and dimeric enzyme have different fluorescence yields. These data and the results of direct binding studies can be explained in terms of a model in which the NADH binding sites on dimeric enzyme are equivalent or nearly equivalent, and NADH binding to monomeric enzyme occurs with an affinity very similar to that of the dimer. However, the fluorescence enhancement of NADH on binding to the enzyme is different for the monomer and for each of the two dimer sites.
R Koren, and
G G Hammes
February 1971,
Biochemistry,
R Koren, and
G G Hammes
August 1979,
Biochemistry,
R Koren, and
G G Hammes
August 1967,
The Biochemical journal,
R Koren, and
G G Hammes
July 1976,
The Biochemical journal,
R Koren, and
G G Hammes
March 1978,
The Biochemical journal,
R Koren, and
G G Hammes
December 1973,
Biochemistry,
R Koren, and
G G Hammes
August 1965,
Nature,
R Koren, and
G G Hammes
August 1965,
Biochimica et biophysica acta,
R Koren, and
G G Hammes
July 1976,
Biochemistry,
R Koren, and
G G Hammes
January 1983,
Veterinarno-meditsinski nauki,
