Binding of ADP to beef-heart mitochondrial ATPase (F1) |
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Authors: | J.P.M. Wielders E.C. Slater J.L.M. Muller |
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Affiliation: | 1. Laboratory of Instrumental Analysis, Eindhoven University of Technology, P.O. Box 513, 5600 MB Eindhoven The Netherlands;2. Laboratory of Biochemistry, B.C.P. Jansen Institute, University of Amsterdam, Plantage Muidergracht 12, 1018 TV Amsterdam The Netherlands |
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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. |
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Keywords: | Mitochondrial ATPase ADP binding Isotachophoresis (Beef heart) mitochondrial ATPase |
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