| Abstract: | An ATPase which strikingly differed from the mitochondrial ATPases of yeast and of animal tissues was obtained when wheat seedling mitochondria, or electron transport particles derived from them, were subjected to ultrasonication and treated with ammonium sulphate. The enzyme which was purified by chromatography on Sephadex G-100 and DEAE-Sephadex (A50) failed to be inactivated as low as 43 000. The enzyme preparation was capable of hydrolysing ADP, in addition to ATP, and several other nucleoside diphosphates and triphosphates. In contrast to the ATPase of animal mitochondria, the activity of the wheat enzyme was almost as insensitive to oligomycin in intact mitochondria as it was after isolation from the organelles. |
