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 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

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.

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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