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

J.P.M. Wielders; E. C. Slater; J.L.M. Muller

doi:10.1016/0005-2728(80)90040-7

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

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

Chemical Engineering and Chemistry

Onderzoeksoutput: Bijdrage aan tijdschrift › Tijdschriftartikel › Academic › peer review

8 Citaten (Scopus)

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Samenvatting

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 (K_d 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.

Originele taal-2	Engels
Pagina's (van-tot)	231-240
Aantal pagina's	10
Tijdschrift	Biochimica et Biophysica Acta, Bioenergetics
Volume	589
Nummer van het tijdschrift	2
DOI's	https://doi.org/10.1016/0005-2728(80)90040-7
Status	Gepubliceerd - 8 feb. 1980

Financiering

The contributions of Dr. O.A. Roveri to the experimental part, and of It. H.N. Linssen and Mr. R. Kool, who did the computer calculations, are gratefully acknowledged. This work was supported by grants from the Netherlands Organization for the Advancement of Pure Research (Z.W.O.), one of which under auspices of the Netherlands Foundation for Chemical Research (S.O.N.).

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10.1016/0005-2728(80)90040-7

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title = "Binding of ADP to beef-heart mitochondrial ATPase (F1)",

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.",

keywords = "(Beef heart), ADP binding, F-ATPase, Isotachophoresis, Mitochondrial ATPase",

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N2 - 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.

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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KW - F-ATPase

KW - Isotachophoresis

KW - Mitochondrial ATPase

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