Journal article
Mitochondrial DNA topoisomerase I from human platelets
Biochimica et biophysica acta, Protein structure and molecular enzymology, v 1078(1)
1991
PMID: 1646636
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
An anucleated cell system has been used for the first time to study mitochondrial topoisomerase activity. Mitochondrial extracts from human blood platelets contained type I topoisomerase. The type I classification was based on ATP-independent activity, inhibition by ATP or camptothecin, and the lack of inhibition by novobiocin. Platelet mitochondrial topoisomerase I relaxation activity was inhibited linearly by increasing concentrations of EGTA. Topoisomerase activity 90% inhibited by 175 μM EGTA was partially restored to 16 and 50% of the initial level of activity by the subsequent addition of 50 and 100 μM Ca
2+, respectively. Additionally, results from studies of partially purified platelet mitochondrial topoisomerase I were consistent with the crude extract data. This work supports the hypothesis that platelet mitochondria contain a type I topoisomerase that is biochemically distinct from that previously isolated and characterized from cell nuclei.
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Details
- Title
- Mitochondrial DNA topoisomerase I from human platelets
- Creators
- Marshall J Kosovsky - Department of Biological Chemistry, Hahnemann University, Philadelphia, PA U.S.AGerald Soslau - Department of Biological Chemistry, Hahnemann University, Philadelphia, PA U.S.A
- Publication Details
- Biochimica et biophysica acta, Protein structure and molecular enzymology, v 1078(1)
- Publisher
- Elsevier
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- [Retired Faculty]
- Web of Science ID
- WOS:A1991FR99200010
- Scopus ID
- 2-s2.0-0025911318
- Other Identifier
- 991014878005404721
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InCites Highlights
Data related to this publication, from InCites Benchmarking & Analytics tool:
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biophysics