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Separation and Characterization of the Subunits of Ribonucleic Acid Polymerase
Open accessAbstract
Abstract This paper presents studies on the subunit structure of Escherichia coli DNA-dependent RNA polymerase. Phosphocellulose column purified enzyme is denatured and its polypeptide chains separated by gel filtration on Sephadex G-200 in the presence of 1% sodium dodecyl sulfate. The amino acid compositions, molecular weights, NH2 terminal amino acids, and molar ratios of these polypeptide chains are presented. It is concluded that phosphocellulose enzyme has the structure α2ββ' where the molecular weights of the chains α, β, and β' are 39,000 ± 5%, 155,000 ± 10%, and 165,000 ± 10%, respectively. In addition, a small protein component, ω, with molecular weight of 9,000 ± 10% is observed. These subunits are not joined together by disulfide linkages. From these data one can compute a molecular weight of 400,000 ± 10% for the monomeric form of the phosphocellulose purified polymerase.
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Cited by
Jishage, M., Iwata, A., Ueda, S., & Ishihama, A. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.18.5447-5451.1996 · Cited by 314
Kimura, H., Tao, Y., Roeder, R. G., & Cook, P. R. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.8.5383 · Cited by 164
Temperature dependence of RNA synthesis parameters in Escherichia coli
Ryals, J., Little, R., & Bremer, H. (1982) · Journal of Bacteriology · doi:10.1128/jb.151.2.879-887.1982 · Cited by 109
Metadata
- Authors
- Burgess, R. R.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1969-11
- Volume
- 244
- Issue
- 22
- Pages
- 6168-6176
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1524162190
- Cited by
- 528
- References
- 0
- FWCI
- 40.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Burgess, R. R. (1969). Separation and Characterization of the Subunits of Ribonucleic Acid Polymerase. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)63521-5
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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