Interaction of reduced nicotinamide adenine dinucleotide with beef heart s-malate dehydrogenase.

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Koren, R; Hammes, GG

Published Date

  • March 11, 1975

Published In

Volume / Issue

  • 14 / 5

Start / End Page

  • 1021 - 1025

PubMed ID

  • 164884

Pubmed Central ID

  • 164884

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00676a021

Language

  • eng

Conference Location

  • United States