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DNA topoisomerase I from human placenta
J A Holden1, D H Rolfson, R L Low
1Department of Pathology, University of Utah, Salt Lake City.
Biochimica Et Biophysica Acta
|July 30, 1990
Summary
Human placenta yields DNA topoisomerase I, an enzyme crucial for DNA repair. This enzyme shows promise for developing and testing novel anticancer drugs targeting topoisomerase I.
Area of Science:
- Biochemistry
- Molecular Biology
- Pharmacology
Background:
- DNA topoisomerase I is essential for managing DNA topology during cellular processes.
- Human placenta is a readily accessible biological source.
Purpose of the Study:
- To investigate human placenta as a source of DNA topoisomerase I.
- To characterize the isolated enzyme and its activity.
- To evaluate its potential in anticancer drug development.
Main Methods:
- Isolation and purification of DNA topoisomerase I from human placenta.
- Chromatographic analysis (phosphocellulose) to resolve enzyme activity.
- Assay of DNA cleavage activity in response to camptothecin.
Main Results:
- Human placenta is an excellent source of intact 100 kDa DNA topoisomerase I.
- Enzyme activity could be resolved into two peaks via phosphocellulose chromatography.
- The enzyme significantly enhanced DNA cleavage in the presence of camptothecin.
Conclusions:
- Human placenta provides a viable source for DNA topoisomerase I isolation.
- The enzyme's activity, particularly its response to camptothecin, makes it valuable.
- This enzyme is a promising tool for developing and testing topoisomerase I-targeting anticancer therapies.