Oligomycin-sensitive ATPase of Submitochondrial Particles from Corn.

To test the hypothesis (Plant Physiology 59: 155-157) that monocotyledons contain a unique oligomycin-insensitive ATPase, we prepared submitochondrial particles and a soluble fraction from sonicated corn mitochondria (Zea mays L. cv. Earliking). Although the ATPase activity of the whole sonicate was relatively insensitive to oligomycin, the corn submitochondrial particles possessed an ATPase activity that was nearly completely inhibited by oligomycin, and was activated by trypsin. This ATPase is similar to that from other sources (plants, animals, and microorganisms). The soluble fraction also contained an active ATPase, which was inhibited by azide and stimulated by sodium chloride and trypsin. The soluble fraction differed from other F(1)-ATPases in that it was cold-stable.