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. 1981 Apr 24;9(8):1949–1961. doi: 10.1093/nar/9.8.1949

Properties of a DNA-dependent ATPase from rat mitochondria.

K Yaginuma, K Koike
PMCID: PMC326815  PMID: 6264401

Abstract

A DNA-dependent ATPase has been highly purified from rat liver mitochondria and characterized. The enzyme catalyzes the hydrolysis of ATP or dATP in the presence of single-stranded DNA cofactor and a divalent cation. The Km values for ATP and dATP are 0.15 mM and 0.35 mM, respectively. The enzyme activity is highly sensitive to N-ethylmaleimide. The sedimentation coefficient of the enzyme is 8.3 S in a glycerol gradient. From this and data on Sephadex G-200 gel filtration, the molecular weight of the native enzyme was calculated to be about 190,000. All the natural single-stranded DNAs tested were equally effective for the ATPase activity, but synthetic deoxyhomopolymer poly(dC) was found to be more effective than natural single-stranded DNAs. Synthetic and natural RNAs had no effect on the activity.

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1960

Selected References

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

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