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. 1982 Feb 15;202(2):453–458. doi: 10.1042/bj2020453

The mitochondrial adenosine triphosphatase of Acanthamoeba castellanii. Oscillatory accumulation of enzyme activity, enzyme protein and F1-inhibitor during the cell cycle.

S W Edwards, J B Evans, J L Williams, D Lloyd
PMCID: PMC1158130  PMID: 6212051

Abstract

1. The mitochondrial ATPase of Acanthamoeba castellanii accumulated discontinuously in synchronous cultures prepared by a minimally perturbing size-selection technique. 2. Enzyme activity per ml of culture doubled overall during one cell cycle time of 8 h, but oscillated to give seven maxima during this period. Similar oscillations were observed in the specific activities of ATPase and of the naturally occurring inhibitor protein. 3. These variations in enzyme activity reflected changes in amount of enzyme protein as assayed by an immunological technique. 4. Large variations in I50 values (micrograms of inhibitor/mg of protein necessary for 50% inhibition of inhibitor-sensitive activity) for inhibition of ATPase activity by seven different inhibitors of energy conservation were observed. Activity was more sensitive to inhibition by oligomycin, efrapeptin, citreoviridin and quercetin when values were highest. 5. The results are discussed in relation to the phased organization of biosynthesis and degradation of cellular components known to occur during the cell cycle of this organization.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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