Calcium-binding ATPase inhibitor protein of bovine heart mitochondria. Role in ATP synthesis and effect of calcium

Biochemistry ◽  
1989 ◽  
Vol 28 (25) ◽  
pp. 9714-9718 ◽  
Author(s):  
Esther W. Yamada ◽  
Norman J. Huzel
Keyword(s):  
Calcium Binding ◽  
Atp Synthesis ◽  
Heart Mitochondria ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Bovine Heart

scholarly journals Functional domains of the ATPase inhibitor protein from bovine heart mitochondria

FEBS Letters ◽  
2000 ◽  
Vol 482 (1-2) ◽  
pp. 163-166 ◽  
Author(s):  
Franco Zanotti ◽  
Gabriella Raho ◽  
Rita Vuolo ◽  
Antonio Gaballo ◽  
Francesco Papa ◽  
...  
Keyword(s):  
Heart Mitochondria ◽  
Functional Domains ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Bovine Heart

The ATPase Inhibitor Protein from Bovine Heart Mitochondria:  The Minimal Inhibitory Sequence†

Biochemistry ◽  
1996 ◽  
Vol 35 (49) ◽  
pp. 15618-15625 ◽  
Author(s):  
Mark J. van Raaij ◽  
George L. Orriss ◽  
Martin G. Montgomery ◽  
Michael J. Runswick ◽  
Ian M. Fearnley ◽  
...  
Keyword(s):  
Heart Mitochondria ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Bovine Heart

scholarly journals Large-scale chromatographic purification of F1F0-ATPase and complex I from bovine heart mitochondria

1996 ◽  
Vol 318 (1) ◽  
pp. 343-349 ◽  
Author(s):  
Susan K BUCHANAN ◽  
John E. WALKER
Keyword(s):  
Complex I ◽  
Large Scale ◽  
Gel Filtration ◽  
Atp Synthesis ◽  
Lipid Vesicles ◽  
Proton Pumping ◽  
Heart Mitochondria ◽  
Nadh:Ubiquinone Oxidoreductase ◽  
Bovine Heart ◽  
F1fo Atpase

A new chromatographic procedure has been developed for the isolation of F1Fo-ATPase and NADH:ubiquinone oxidoreductase (complex I) from a single batch of bovine heart mitochondria. The method employed dodecyl β-Δ-maltoside, a monodisperse, homogeneous detergent in which many respiratory complexes exhibit high activity, for solubilization and subsequent purification by ammonium sulphate fractionation and column chromatography. A combination of anion-exchange, gel-filtration, and dye-ligand affinity chromatography was used to purify both complexes to homogeneity. The F1Fo-ATPase preparation contains only the 16 known subunits of the enzyme. It has oligomycin-sensitive ATP hydrolysis activity and, as demonstrated elsewhere, when reconstituted into lipid vesicles it is capable of ATP-dependent proton pumping and of ATP synthesis driven by a proton gradient [Groth and Walker (1996) Biochem. J. 318, 351–357]. The complex I preparation contains all of the subunits identified in other preparations of the enzyme, and has rotenone-sensitive NADH:ubiquinone oxidoreductase and NADH:ferricyanide oxidoreductase activities. The procedure is rapid and reproducible, yielding 50–80 mg of purified F1Fo-ATPase and 20–40 mg of purified complex I from 1 g of mitochondrial membranes. Both preparations are devoid of phospholipids, and gel filtration and dynamic light scattering experiments indicate that they are monodisperse. Therefore, the preparations fulfil important prerequisites for structural analysis.

scholarly journals The adenosine triphosphatase-inhibitor content of bovine heart submitochondrial particles. Influence of the inhibitor on adenosine triphosphate-dependent reactions

1977 ◽  
Vol 162 (2) ◽  
pp. 351-357 ◽  
Author(s):  
S J Ferguson ◽  
D A Harris ◽  
G K Radda
Keyword(s):  
Atpase Activity ◽  
Adenosine Triphosphatase ◽  
Type I ◽  
Type Ii ◽  
Inhibitor Protein ◽  
Isolation Method ◽  
Atpase Inhibitor ◽  
Submitochondrial Particles ◽  
Bovine Heart ◽  
Tightly Bound Nucleotides

1. The activity of the ATPase (adenosine triphosphatase) of phosphorylating particles prepared by sonication of bovine heart mitochondria in the presence of MgCl2 and ATP is influenced by the isolation method for the mitochondria used in the preparation of particles. Type-I particles, made from mitochondria isolated in a medium lacking succinate, have a lower ATPase activity than to Type-II particles, which are prepared from mitochondria isolated in a medium containing succinate. 2. Centrifugation under appropriate energized conditions increases the ATPase activity of Type-I particles almost to that of the Type-II particles. The ATPase activity of Type-II particles was only slightly stimulated by this procedure. These data are interpreted as indicating a higher content of the ATPase-inhibitor protein in the Type-I particles. 3. A comparison was made of the ATP-driven enhancement of 8-anilinonaphthalene-1-sulphonate fluorescence and the exchange of the endogenous tightly bound nucleotides of the ATPase in Type-I and Type-II particles. The effect of exogenous inhibitor protein on both these reactions was also studied. 4. The time-scale on which the inhibitor protein can exchange between ATPase molecules is discussed.

Binding of mitochondrial ATPase from ox heart to its naturally occurring inhibitor protein: Localization by antibody binding

1983 ◽  
Vol 3 (10) ◽  
pp. 921-926 ◽  
Author(s):  
Philip J. Jackson ◽  
David A. Harris
Keyword(s):  
Binding Site ◽  
Protein Localization ◽  
Antibody Binding ◽  
Heart Mitochondria ◽  
Mitochondrial Atpase ◽  
Β Subunit ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Naturally Occurring ◽  
The Cross

The naturally occurring ATPase inhibitor protein from ox heart mitochondria was cross-linked to its binding site on the mitochondrial ATPase using 1-ethyl-3-(dimethylamino)propyl carbodiimide. The cross-linked product, when transferred electrophoretically to a nitrocellulose sheet, reacted with antibodies directed against the inhibitor protein and the β-subunit of the ATPase. It was concluded that the binding site for the inhibitor protein lies on the β-subunit.

Synthesis and hydrolysis of ATP by the mitochondrial ATP synthase

1988 ◽  
Vol 66 (7) ◽  
pp. 677-682 ◽  
Author(s):  
M. Tuena de Gômez-Puyou ◽  
Orlando B. Martins ◽  
A. Gômez-Puyou
Keyword(s):  
Atp Synthase ◽  
Atp Hydrolysis ◽  
Atp Synthesis ◽  
Control Synthesis ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
Mitochondrial Atp Synthase ◽  
High Concentrations ◽  
Hydrolysis Of

A brief summary of the factors that control synthesis and hydrolysis of ATP by the mitochondrial H+-ATP synthase is made. Particular emphasis is placed on the role of the natural ATPase inhibitor protein. It is clear from the existing data obtained with a number of agents that there is no correlation between variations of the rate of ATP hydrolysis and ATP synthesis as driven by respiration. The mechanism by which each condition differentially affects the two activities is not entirely known. For the case of the natural ATPase inhibitor protein, it appears that the protein controls the kinetics of the enzyme. This control seems essential for achieving maximal accumulation of ATP during electron transport in systems that contain relatively high concentrations of ATP.

Recombinant bovine heart mitochondrial F1-ATPase inhibitor protein: Overproduction in Escherichia coli, purification, and structural studies

Biochemistry ◽  
1993 ◽  
Vol 32 (38) ◽  
pp. 10140-10149 ◽  
Author(s):  
Gino Van Heeke ◽  
Lily Deforce ◽  
Richard A. Schnizer ◽  
Regina Shaw ◽  
Judy M. Couton ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Structural Studies ◽  
Inhibitor Protein ◽  
Atpase Inhibitor ◽  
F1 Atpase ◽  
Bovine Heart ◽  
Protein Overproduction
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