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FEBS Lett ; 218(1): 163-6, 1987 Jun 22.
Article in English | MEDLINE | ID: mdl-3109946

ABSTRACT

RNA polymerase from Streptomyces aureofaciens has been purified by polyethyleneimine precipitation followed by chromatography first on DEAE-cellulose, then heparin-Sepharose and finally on an aminooxybutylcellulose matrix containing immobilised S. aureofaciens DNA. The enzyme is composed of three subunits of approximately 145, 136 and 44 kDa that are in a ratio of approx. 1:1:2. In many isolations two additional subunits of approximately 68 and 39 kDa and some minor protein bands of approximately 110, 85 and 61 kDa are also present. Thus, the structure of this enzyme is very similar to other bacterial RNA polymerases, exhibiting an alpha 2 beta beta' core and the additional proteins rho and sigma.


Subject(s)
DNA-Directed RNA Polymerases/isolation & purification , Fungal Proteins/isolation & purification , Streptomyces aureofaciens/enzymology , Chlortetracycline/biosynthesis , Chromatography, Affinity , Chromatography, DEAE-Cellulose , DNA-Directed RNA Polymerases/metabolism , Fungal Proteins/metabolism , Protein Conformation , Substrate Specificity , Transcription, Genetic
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