Difference between revisions of "Pullman 1960 J Biol Chem"
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{{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 | ||
|year=1960 | |year=1960 | ||
|journal=J Biol Chem | |journal=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 4°. 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. | |||
|keywords=Oxidative phosphorylation, Enzymes, Dinitrophenol, ATP, Beef heart | |||
}} | }} | ||
{{Labeling | {{Labeling | ||
|organism=Bovines | |||
|tissues=Heart | |||
|preparations=Isolated mitochondria | |||
|enzymes=Complex V;ATP synthase | |||
|topics=ATP, Temperature | |||
|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 4°. 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.
• 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
