Pullman 1960 J Biol Chem
From Bioblast
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 235:3322-9. |
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 4Β°. 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.
β’ Keywords: Oxidative phosphorylation, Enzymes, Dinitrophenol, ATP, Beef heart
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex V;ATP synthase
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., Temperature
Coupling state: OXPHOS
Made history