STUDIES ON MITOCHONDRIAL ADENOSINE TRIPHOSPHATASE SYSTEM .4. PURIFICATION AND CHARACTERIZATION OF OLIGOMYCIN SENSITIVITY CONFERRING PROTEIN

A soluble protein of mol wt 18,000, isolated in highly purified form, has been shown to control the sensitivity of the mitochondrial ATPase to oligomycin. The protein also restores energy-linked functions of A particles to which F1 has been rebound. In these respects the protein appears to correspond to the active component in the crude fraction designated as F4 by Conover and coworkers (Conover, T. E., Prairie, R. L., and Racker, E. (1963), J. Biol. Chem. 238, 2831). The purified protein is, however, at least 240 times more active than the F4 preparation. The protein has been shown not to be present in the oligomycin-insensitive ATPase (F1) but is a component of the oligomycin-sensitive ATPase complex. The oligomycin sensitivity conferring protein has been chosen as the designation for the purified enzyme. © 1968, American Chemical Society. All rights reserved.