Solubilization of mitochondrial ATPase by phospholipids

Brief incubation of submitochondrial particles from bovine-heart with the acidic phospholipid, diphosphatidylglycerol (cardiolipin), resulted in the solubilization of mitochondrial ATPase (F 1). Little or no effect was evident with submitochondrial particles from rat-liver. The solubilized ATPase was oligomycin insensitive, cold labile and showed the same electrophoretic pattern as pure F 1. The specific activity and the polyacrylamide gel electrophoresis indicated that mitochondrial ATPase is extracted in a considerable degree of purity. Other phospholipids partially reproduced the effect of diphosphatidylglycerol whereas some anionic or non ionic detergents were ineffective under the same conditions.