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The mitochondrial atp of acanthamoeba castellanii partial characterization and changes in activity during exponential growth






Comparative Biochemistry & Physiology B 71(3): 495-500

The mitochondrial atp of acanthamoeba castellanii partial characterization and changes in activity during exponential growth

The mitochondrial ATPase of A. castellanii is Mg2+-requiring (optimum cation: ATP ratio of 1.5) and has 2 pH optima of activity (at pH 6.6 and 8.1). ATPase activity of submitochondrial particles is effectively inhibited by 12 different inhibitors of energy conservation suggesting similarities in inhibitor-binding sites to other previously characterized complexes. Gel filtration by passage through Sephadex G-50 increases ATPase activity of submitochondrial particles between 1.5-3.5 fold indicating the presence of a low MW inhibitor protein. After removal of the inhibitor protein, sensitivity to inhibitors of energy conservation decreases by between 1.5-14 fold. Crude F1-inhibitor preparations from A. castellanii, Schizosaccharomyces pombe, Tetranymena pyriformis and bovine heart also inhibit ATPase activity. Large variations in ATPase activity, F1-inhibitor protein activity and amounts of immunologically-determined ATPase protein were observed during exponential growth and the correlation between changes in these measurements is discussed. The results are also discussed highlighting the similarities between the mitochondrial ATPase of A. castellanii and other mitochondrial ATPases.

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Accession: 006719057



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