Preparation and general properties of a soluble adenosine triphosphatase from mitochondria.
1. The purification of an adenosine triphosphatase present in aqueous extracts of acetone-dried ox-heart mitochondria is described. 2. No evidence was found for the presence of more than one protein having adenosine-triphosphatase activity in these extracts. 3. The enzyme is less stable at 0 degrees than at 25 degrees but is stabilized by glycerol. 4. The activity is dependent on the presence of Mg(2+) or certain other bivalent metal cations. 5. The adenosine-triphosphatase activity of the Mg(2+)-activated enzyme is enhanced by 2,4-dinitrophenol. 6. The kinetics of Mg(2+) activation indicate that the ATP-Mg(2+) complex is the important substrate: free ATP and Mg(2+) are inhibitory. 7. This preparation of mitochondrial adenosine triphosphatase has many properties in common with the adenosine triphosphatase coupling factor from mitochondria (Racker, 1961).
D000096:Acetone; D000251:Adenosine Triphosphatases / Q000032:analysis*; D000255:Adenosine Triphosphate; D000818:Animals; D002417:Cattle; D002482:Cellulose; D011232:Chemical Precipitation; D002845:Chromatography; D002850:Chromatography, Gel; D004586:Electrophoresis; D007700:Kinetics; D008274:Magnesium; D008931:Mitochondria, Muscle / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D012995:Solubility; D013696:Temperature
D000096:Acetone; D000255:Adenosine Triphosphate; D002482:Cellulose; D000251:Adenosine Triphosphatases; D008274:Magnesium