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Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation

IX. RECONSTRUCTION OF OLIGOMYCIN-SENSITIVE ADENOSINE TRIPHOSPHATASE

From the ¹ From the Department of Biochemistry, The Public Health Research Institute of the City of New York, Inc., New York, New York 10009

1. A factor conferring oligomycin sensitivity on mitochondrial ATPase was obtained from submitochondrial particles by sequential treatment with trypsin and urea, and was purified by fractionation with ammonium sulfate in the presence of 2% cholate. The preparation had a very low content of phospholipids and respiratory enzymes.

2. By omitting treatment with urea, an insoluble, oligomycin-sensitive ATPase was isolated which was also low in respiratory enzymes and phospholipids.

3. Addition of soluble mitochondrial ATPase to the factor conferring oligomycin sensitivity resulted in a marked inhibition of ATPase activity, which was fully restored by addition of phospholipids. Similarly, the isolated oligomycin-sensitive ATPase required phospholipids for ATPase activity.

4. The interaction of these preparations with tritium-labeled ATPase, ¹⁴C-phospholipids and ¹⁴C-rutamycin was analyzed quantitatively. The binding capacity of the factor for ³H-labeled ATPase was much larger than that of various particles containing phospholipids. Addition of phospholipids interfered with the binding of ³H-labeled ATPase. Inhibition by ¹⁴C-rutamycin was reversed by repeated washing of particles with phospholipids.

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