Thermostable polynucleotide phosphorylases from Bacillus stearothermophilus and Thermus aquaticus.
Polynucleotide phosphorylase from Bacillus stearothermophilus has been purified to homogeneity. Polyacrylamide gel electrophoresis run under denaturing conditions indicates that the enzyme is a tetramer with subunits of apparent molecular weight 51,000 daltons. A partial purification of polynucleoti...
שמור ב:
| הוצא לאור ב: | Nucleic Acids Res |
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| Principais autores: | , |
| פורמט: | Artigo |
| שפה: | Inglês |
| יצא לאור: |
Oxford University Press
1976
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| גישה מקוונת: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC342889/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/1250699/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/nar/3.1.219 |
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