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

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.

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A simple and rapid method for the preparation of adenosine triphosphatase from submitochondrial particles

Biochemical Journal ◽

10.1042/bj1480533 ◽

1975 ◽

Vol 148 (3) ◽

pp. 533-537 ◽

Cited By ~ 214

Author(s):

R B Beechey ◽

S A Hubbard ◽

P E Linnett ◽

A D Mitchell ◽

E A Munn

Keyword(s):

Electron Microscopy ◽

Rapid Method ◽

Adenosine Triphosphatase ◽

Pure Form ◽

Heart Mitochondria ◽

Polyacrylamide Gels ◽

Submitochondrial Particles ◽

Bovine Heart

An almost pure form of the bovine heart mitochondrial adenosine triphosphatase (ATPase) is released from the membrane by shaking submitochondrial particles with chloroform. Analyses on polyacrylamide gels and by electron microscopy, and also sensitivity to inhibitors, show that the chloroform-released enzyme is similar to other ATPase preparations from bovine heart mitochondria.

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Involvement of the endogenous inhibitor protein in the MgATP-induced inhibition of soluble mitochondrial adenosine triphosphatase activity

Biochemical Journal ◽

10.1042/bj2000655 ◽

1981 ◽

Vol 200 (3) ◽

pp. 655-661 ◽

Cited By ~ 3

Author(s):

P N Lowe ◽

R B Beechey

Keyword(s):

Atpase Activity ◽

Adenosine Triphosphatase ◽

Heart Mitochondria ◽

Inhibitor Protein ◽

Endogenous Inhibitor ◽

Adenosine Triphosphatase Activity

Chloroform-released ATPase from ox heart mitochondria contains significant amounts of inhibitor protein. There is a correlation between processes that affect the interactions between the inhibitor protein and the ATPase molecule and the ability of MgATP to induce an inhibition of ATPase activity. Evidence is presented suggesting that the endogenous inhibitor protein is involved in the process of MgATP-induced inhibition of soluble ATPase activity.

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A comparison of membrane-bound enzymes of the isolated brush border plasma membranes of the cestodes Hymenolepis diminuta and H. microstoma

Parasitology ◽

10.1017/s0031182000044930 ◽

1982 ◽

Vol 84 (2) ◽

pp. 391-396 ◽

Cited By ~ 8

Author(s):

P. W. Pappas ◽

Elizabeth M. Narcisi

Keyword(s):

Brush Border ◽

Adenosine Triphosphatase ◽

Plasma Membranes ◽

Leucine Aminopeptidase ◽

Enzymatic Activities ◽

Hymenolepis Diminuta ◽

Type I ◽

Type Ii ◽

Membrane Bound ◽

Membrane Bound Enzymes

SUMMARYPreparations of isolated brush border plasma membrane of Hymenolepis diminuta and H. microstoma possess the following enzymatic activities: alkaline phosphohydrolase (E.C. 3.1.3.1); Type I phosphodiesterase (E.C. 3.1.4.1); ribonuclease (E.C. 3.1.4.22); adenosine triphosphatase (E.C. 3.6.1.3); and 5′-nucleotidase (E.C. 3.1.3.5). The following enzymatic activities could not be demonstrated in either membrane preparation: Type II phosphodiesterase (E.C. 3.1.4.18); cyclic adenosine-3′, 5′-monophosphate phosphodiesterase (E.C. 3.1.4.17); leucine aminopeptidase (E.C. 3.4.11.1); maltase (α-glucosidase; E.C. 3.2.1.20); and lactase (β-galactosidase; E.C. 3.2.1.23). These data generally agree with those of previous studies in which similar membrane-bound enzymes were demonstrated in intact (living) worms.

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Functional domains of the ATPase inhibitor protein from bovine heart mitochondria

FEBS Letters ◽

10.1016/s0014-5793(00)02055-x ◽

2000 ◽

Vol 482 (1-2) ◽

pp. 163-166 ◽

Cited By ~ 5

Author(s):

Franco Zanotti ◽

Gabriella Raho ◽

Rita Vuolo ◽

Antonio Gaballo ◽

Francesco Papa ◽

...

Keyword(s):

Heart Mitochondria ◽

Functional Domains ◽

Inhibitor Protein ◽

Atpase Inhibitor ◽

Bovine Heart

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

Biochemistry ◽

10.1021/bi960628f ◽

1996 ◽

Vol 35 (49) ◽

pp. 15618-15625 ◽

Cited By ~ 50

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

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Mitochondrial adenosine triphosphatase of the fission yeast, Schizosaccharomyces pombe 972h-. Changes in activity and inhibitor-sensitivity in response to catabolite repression

Biochemical Journal ◽

10.1042/bj1600335 ◽

1976 ◽

Vol 160 (2) ◽

pp. 335-342 ◽

Cited By ~ 12

Author(s):

D Lloyd ◽

S W Edwards

Keyword(s):

Atpase Activity ◽

Schizosaccharomyces Pombe ◽

Adenosine Triphosphatase ◽

Specific Activity ◽

Early Stage ◽

Gel Filtration ◽

Growth Cycle ◽

Mitochondrial Atpase ◽

Submitochondrial Particles ◽

Fourfold Increase

1. The specific activity of mitochondrial ATPase (adenosine triphosphatase) in extracts of Schizosaccharomyces pombe decreased 2.5-fold as the glucose concentration in the growth medium decreased from 50mM to 15mM. 2. During the late exponential phase of growth, ATPase activity doubled. 3. Sensitivity to oligomycin and Dio-9 as measured by values for I50(mug of inhibitor/mg of protein giving 50% inhibition) at pH 6.8 increased sixfold and ninefold respectively during the initial decrease in ATPase activity, and this degree of sensitivity was maintained for the remainder of the growth cycle. 4. Increased sensitivity to NN′-dicyclohexylcarbodi-imide, triethyltin and venturicidin was also observed during the early stage of glucose de-repression. 5. Smaller increases in sensitivity to efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diaz-le, quercetin and spegazzinine also occurred. 6. The ATPase of glycerol-grown cells was less sensitive to inhibitors than that of glucose-repressed cells; change in values for I50 were not so marked during the growth cycle of cells growing with glycerol. 7. When submitochondrial particles from glycerol-grown cells were tested by passage through Sephadex G-50, a fourfold increase in activity was accompanied by increased inhibitor resistance. 8. Gel filtration of submitochondrial particles from glucose-de-repressed cells gave similar results, whereas loss of ATPase occurred in submitochondrial particles from glucose-repressed cells. 9. It is proposed that alterations in sensitivity to inhibitors at different stages of glucose derepression may be partly controlled by a naturally occuring inhibitor of ATPase. 10. The inhibitors tested may be classififed into two groups on the basis of alterations of sensitivity of the ATPase during physiological modification: (a) oligomycin, Dio-9, NN′-dicyclohexylcarbodi-imide, venturicidin and triethyltin, and (b) efrapeptin, aurovertin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole, quercetin and spegazzinine.

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