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

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

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Abstract

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
Volume589
Issue number2
DOIs
Publication statusPublished - 8 Feb 1980

Fingerprint

Beef
Proton-Translocating ATPases
Adenosine Diphosphate
Binding Sites
Ultrafiltration
Adenosine Triphosphate
Ligands
Red Meat
Experiments

Keywords

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

Cite this

Wielders, J.P.M. ; Slater, E. C. ; Muller, J.L.M. / Binding of ADP to beef-heart mitochondrial ATPase (F1). In: Biochimica et Biophysica Acta, Bioenergetics. 1980 ; Vol. 589, No. 2. pp. 231-240.
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Binding of ADP to beef-heart mitochondrial ATPase (F1). / Wielders, J.P.M.; Slater, E. C.; Muller, J.L.M. (Corresponding author).

In: Biochimica et Biophysica Acta, Bioenergetics, Vol. 589, No. 2, 08.02.1980, p. 231-240.

Research output: Contribution to journalArticleAcademicpeer-review

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AB - 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.

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