Purification of DNA-dependent RNA polymerase from Streptomyces granaticolor
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články
PubMed
6642321
DOI
10.1007/bf02879496
Knihovny.cz E-zdroje
- MeSH
- bakteriální proteiny analýza MeSH
- chemická precipitace MeSH
- chromatografie afinitní MeSH
- DNA řízené RNA-polymerasy analýza izolace a purifikace MeSH
- elektroforéza v polyakrylamidovém gelu MeSH
- gelová chromatografie MeSH
- Streptomyces enzymologie MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- bakteriální proteiny MeSH
- DNA řízené RNA-polymerasy 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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Nature. 1970 Aug 15;227(5259):680-5 PubMed
Arch Biochem Biophys. 1979 Nov;198(1):195-204 PubMed
FEBS Lett. 1980 Nov 3;120(2):233-5 PubMed
Nucleic Acids Res. 1981 Jul 10;9(13):3129-38 PubMed
Biochem Biophys Res Commun. 1978 Oct 30;84(4):962-8 PubMed
Biochem Biophys Res Commun. 1976 Sep 20;72(2):522-9 PubMed
Biochemistry. 1976 Jul 27;15(15):3331-41 PubMed
Isolation of DNA-dependent RNA polymerase from the thermophilic actinomycete Thermomonospora curvata
Some properties of DNA-dependent RNA polymerase from Streptomyces granaticolor
Transformation of Streptomyces granaticolor with natural and recombinant plasmid vectors
