Purification of DNA-dependent RNA polymerase from Streptomyces granaticolor
Language English Country United States Media print
Document type Journal Article
PubMed
6642321
DOI
10.1007/bf02879496
Knihovny.cz E-resources
- MeSH
- Bacterial Proteins analysis MeSH
- Chemical Precipitation MeSH
- Chromatography, Affinity MeSH
- DNA-Directed RNA Polymerases analysis isolation & purification MeSH
- Electrophoresis, Polyacrylamide Gel MeSH
- Chromatography, Gel MeSH
- Streptomyces enzymology MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- Bacterial Proteins MeSH
- DNA-Directed RNA Polymerases MeSH
RNA nucleotidyltransferase (EC 2.7.7.6) of Streptomyces granaticolor was purified by precipitation with polymin P and ammonium sulphate, affinity chromatography on DNA- cellulose and gell filtration on Biogel A 1.5 m. SDS-polyacrylamide gel electrophoresis revealed 8 protein bands of molar mass ranging from 37 to 130 kg/mol. Proteins of molar mass of 130 and 120 kg/mol were identified to be beta and beta subunits, respectively. The role of other subunits of the enzyme is discussed.
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