Pullman 1960 J Biol Chem: Difference between revisions
From Bioblast
No edit summary |
No edit summary ย |
||
(6 intermediate revisions by 4 users not shown) | |||
Line 1: | Line 1: | ||
{{Publication | {{Publication | ||
|title=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- | |title=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. | ||
|info=[http://www.jbc.org/content/235/11/3322.full.pdf+html PMID: 13738472 Open Access] | |info=[http://www.jbc.org/content/235/11/3322.full.pdf+html PMID: 13738472 Open Access] | ||
|authors=Pullman ME, Penefsky HS, Datta A, Racker E | |authors=Pullman ME, Penefsky HS, Datta A, Racker E | ||
Line 12: | Line 12: | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism= | |organism=Bovines | ||
|tissues= | |tissues=Heart | ||
|preparations=Isolated | |preparations=Isolated mitochondria | ||
|enzymes=Complex V;ATP synthase | |||
|topics=ATP, Temperature | |||
|couplingstates=OXPHOS | |couplingstates=OXPHOS | ||
|additional=Made history | |additional=Made history | ||
}} | }} |
Latest revision as of 16:09, 25 November 2015
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 4ยฐ. 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.
โข Keywords: Oxidative phosphorylation, Enzymes, Dinitrophenol, ATP, Beef heart
Labels:
Organism: Bovines
Tissue;cell: Heart
Preparation: Isolated mitochondria
Enzyme: Complex V;ATP synthase
Regulation: ATP, Temperature
Coupling state: OXPHOS
Made history