Pullman 1960 J Biol Chem

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.

» PMID: 13738472 Open Access

Pullman ME, Penefsky HS, Datta A, Racker E (1960) J Biol Chem

Abstract:

1. 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.
2. The enzyme is cold labile. Although stable at room temperature, the enzyme rapidly loses activity at 4°. ATP, which protects the enzyme against inactivation by heat and dialysis, does not prevent the cold inactivation.
3. Attempts to demonstrate an exchange between either Pi32 or C14-ADP and ATP in the presence of the enzyme were unsuccessful.
4. The properties of the purified enzyme are discussed in relation to particulate mitochondrial ATPase and to myosin ATPase.

• 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 

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