Heat-labile alkaline phosphatase from Antarctic bacteria: Rapid 5′ end-labeling of nucleic acids
A heat-labile alkaline phosphatase has been purified to near homogeneity from HK47, a bacterial strain isolated from Antarctic seawater. The active form of the enzyme has a molecular weight of 68,000 and is uniquely monomeric. The optimal temperature for the enzymatic activity is 25°C. Complete and...
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| Vydáno v: | Proc Natl Acad Sci U S A |
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| Hlavní autoři: | , , |
| Médium: | Artigo |
| Jazyk: | Inglês |
| Vydáno: |
National Academy of Sciences
1984
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| Témata: | |
| On-line přístup: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC391996/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/16593525/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.81.21.6691 |
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