Difference between revisions of "Pullman 1960 J Biol Chem"
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# AttemptsĀ toĀ demonstrateĀ anĀ exchangeĀ betweenĀ eitherĀ Pi32 orĀ C14-ADPĀ andĀ ATPĀ inĀ theĀ presenceĀ ofĀ theĀ enzymeĀ wereĀ unsuccessful. Ā | # AttemptsĀ toĀ demonstrateĀ anĀ exchangeĀ betweenĀ eitherĀ Pi32 orĀ C14-ADPĀ andĀ ATPĀ inĀ theĀ presenceĀ ofĀ theĀ enzymeĀ wereĀ unsuccessful. Ā | ||
# TheĀ propertiesĀ ofĀ theĀ purifiedĀ enzymeĀ areĀ discussedĀ in relationĀ toĀ particulateĀ mitochondrialĀ ATPaseĀ andĀ toĀ myosin ATPase. | # TheĀ propertiesĀ ofĀ theĀ purifiedĀ enzymeĀ areĀ discussedĀ in relationĀ toĀ particulateĀ mitochondrialĀ ATPaseĀ andĀ toĀ myosin ATPase. | ||
|keywords=oxidative phosphorylation, enzymes, dinitrophenol, ATP | |keywords=oxidative phosphorylation, enzymes, dinitrophenol, ATP | ||
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|tissues=Cardiac muscle | |tissues=Cardiac muscle | ||
|preparations=Isolated Mitochondria | |preparations=Isolated Mitochondria | ||
|couplingstates=OXPHOS | |||
|enzymes=Complex V; ATP Synthase | |enzymes=Complex V; ATP Synthase | ||
|kinetics=Temperature | |kinetics=Temperature | ||
|topics= | |topics=ATP; ADP; AMP; PCr | ||
|additional=Made history | |additional=Made history | ||
}} | }} | ||
Revision as of 16:20, 27 November 2012
| Pullman ME, Penefsky HS, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble dinitrophenol-stimulated adenosine triphosphatase. J Biol Chem 235: 3322-3329. |
Pullman ME, Penefsky HS, Datta A, Racker E (1960) J Biol Chem
Abstract:
- The purification o f a soluble ATPase from beef heart mitochondria is described. The activity is dependent on Mg++ and is stimulated by 2,4-dinitrophenol. The enzyme cleaves the terminal phosphate of ATP and is inhibited by ADP. The activity is therefore assayed in the presence of an ATP regenerating system.
- The enzyme is cold labile. Although stable at room temperature, the enzyme rapidly loses activity at 4Ā°. ATP, which protects the enzyme against inactivation by heat and dialysis, does not prevent the cold inactivation.
- Attempts to demonstrate an exchange between either Pi32 or C14-ADP and ATP in the presence of the enzyme were unsuccessful.
- The properties of the purified enzyme are discussed in relation to particulate mitochondrial ATPase and to myosin ATPase.
ā¢ Keywords: oxidative phosphorylation, enzymes, dinitrophenol, ATP
Labels:
Organism: Other Mammal"Other Mammal" is not in the list (Human, Pig, Mouse, Rat, Guinea pig, Bovines, Horse, Dog, Rabbit, Cat, ...) of allowed values for the "Mammal and model" property.
Tissue;cell: Cardiac muscle"Cardiac muscle" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.
Preparation: Isolated Mitochondria"Isolated Mitochondria" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Enzyme: Complex V; ATP Synthase"Complex V; ATP Synthase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
Regulation: ATP; ADP; AMP; PCr"ATP; ADP; AMP; PCr" is not in the list (Aerobic glycolysis, ADP, ATP, ATP production, AMP, Calcium, Coupling efficiency;uncoupling, Cyt c, Flux control, Inhibitor, ...) of allowed values for the "Respiration and regulation" property.
Coupling state: OXPHOS
Made history
