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Partial Resolution of the Enzymes Catalyzing Oxidative Phosphorylation

VIII. PROPERTIES OF A FACTOR CONFERRING OLIGOMYCIN SENSITIVITY ON MITOCHONDRIAL 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. The properties of a mitochondrial fraction (F₀) which confers oligomycin sensitivity on soluble ATPase were found to resemble in several aspects the properties of particles that catalyze oxidative phosphorylation. Susceptibility to oligomycin, Dio-9, tri-n-butyltin chloride, detergents, and phospholipase A are shared by both systems.

2. Treatment of F₀ with phospholipase A resulted in complete loss of activity. About half of the original activity was restored by treatment of the preparation with serum albumin and phospholipids.

3. Brief exposure of particles containing F₀ activity to trypsin or to sonic oscillation either at pH 10.0 or in the presence of phospholipid resulted in partial loss of F₀ activity. Full restoration of activity was achieved by addition of coupling factor 4.

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