pubmed-article:7431488 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7431488 | lifeskim:mentions | umls-concept:C2247630 | lld:lifeskim |
pubmed-article:7431488 | lifeskim:mentions | umls-concept:C0597177 | lld:lifeskim |
pubmed-article:7431488 | lifeskim:mentions | umls-concept:C0614315 | lld:lifeskim |
pubmed-article:7431488 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:7431488 | pubmed:dateCreated | 1981-1-16 | lld:pubmed |
pubmed-article:7431488 | pubmed:abstractText | We previously reported that virus-specific particles with polycytidylate [poly(C)]-dependent RNA polymerase activity accumulated at 30 degrees C in reovirus-infected cells. These particles sedimented heterogeneously from 300 to 550S and traversed through a 40% glycerol cushion to the pellet in 3 h at 190,000 x g. In the present report, we found that smaller particles with poly(C)-dependent RNA polymerase activity remained in the glycerol cushion. These smaller, enzymatically active particles, when purified, sedimented at 15 to 1S. They were spherical or triangular with a diameter of 11 to 12 nm. They were comprised mostly, and likely solely, of one reovirus protein, sigma NS. No particles with poly(C)-dependent RNA polymerase activity were found in mock-infected cells. Chromatography on the cation exchanger, CM-Sephadex, ascertained that sigma NS was the poly(C)-dependent RNA polymerase and showed its existence in two forms. In one form, it was enzymatically active and eluted from the column at 0.5 M KCl. In the enzymatically inactive state, it did not bind to the column. Our results suggest that the enzymatically active form of sigma NS carries a greater net positive charge than the inactive form. They also suggest that both forms of sigma NS are associated with a particle which has poly(C)-dependent RNA polymerase activity. | lld:pubmed |
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pubmed-article:7431488 | pubmed:language | eng | lld:pubmed |
pubmed-article:7431488 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7431488 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:7431488 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7431488 | pubmed:month | Nov | lld:pubmed |
pubmed-article:7431488 | pubmed:issn | 0022-538X | lld:pubmed |
pubmed-article:7431488 | pubmed:author | pubmed-author:SarkarN HNH | lld:pubmed |
pubmed-article:7431488 | pubmed:author | pubmed-author:GomatosP JPJ | lld:pubmed |
pubmed-article:7431488 | pubmed:author | pubmed-author:StamatosN MNM | lld:pubmed |
pubmed-article:7431488 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7431488 | pubmed:volume | 36 | lld:pubmed |
pubmed-article:7431488 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7431488 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7431488 | pubmed:pagination | 556-65 | lld:pubmed |
pubmed-article:7431488 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:7431488 | pubmed:year | 1980 | lld:pubmed |
pubmed-article:7431488 | pubmed:articleTitle | Small reovirus-specific particle with polycytidylate-dependent RNA polymerase activity. | lld:pubmed |
pubmed-article:7431488 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:7431488 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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