Binding of ADP to beef-heart mitochondrial ATPase (F1)

J.P.M. Wielders, E. C. Slater, J.L.M. Muller (Corresponding author)

Research output: Contribution to journalArticleAcademicpeer-review

84 Downloads (Pure)


1. ADP binding to beef-heart mitochondrial ATPase (F1), in the absence of Mg2+, has been determined by separating the free ligand by ultrafiltration and determining it in the filtrate by a specially modified isotachophoretic procedure. 2. Since during the binding experiments the 'tightly' bound ADP (but not the ATP) dissociates, it is necessary to take this into account in calculating the binding parameters. 3. The binding data show that only one tight binding site (Kd about 0.5 μM) for ADP is present. 4. It is not possible to calculate from the binding data alone the number of or the dissociation constants for the weak binding sites. It can be concluded, however, that the latter is not less than about 50 μM.

Original languageEnglish
Pages (from-to)231-240
Number of pages10
JournalBiochimica et Biophysica Acta, Bioenergetics
Issue number2
Publication statusPublished - 8 Feb 1980


  • (Beef heart)
  • ADP binding
  • F-ATPase
  • Isotachophoresis
  • Mitochondrial ATPase


Dive into the research topics of 'Binding of ADP to beef-heart mitochondrial ATPase (F1)'. Together they form a unique fingerprint.

Cite this