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Characterization of a prokaryotic topoisomerase I activity in chloroplast extracts from spinach.
A topoisomerase I activity has been partially purified from crude extracts of spinach chloroplasts. This activity relaxes the supercoiled covalently closed circular DNA of pBR322. The enzyme requires Mg++, but not ATP, and has an apparent molecular weight of about 115,000. It catalyzes a unit change...
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| Vydáno v: | Nucleic Acids Res |
|---|---|
| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
Oxford University Press
1983
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| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC325812/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6298746/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/11.5.1523 |
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