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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1972 Dec;69(12):3815–3819. doi: 10.1073/pnas.69.12.3815

Isolation and Subunit Structure of Polycytidylate-Dependent RNA Polymerase of Encephalomyocarditis Virus

H Rosenberg 1,2, B Diskin 1,2, L Oron 1,2, A Traub 1,2
PMCID: PMC389880  PMID: 4345509

Abstract

A polycytidylate-dependent RNA polymerase of encephalomyocarditis virus was isolated from infected BHK 21 cells. The enzyme was associated with a smooth-membrane fraction, from which it was extracted by a mixture of sodium dodecyl sulfate, Triton X-100, and dithiothreitol, and further purified by chromatography on a Dowex-1 column and by glycerol gradient sedimentation. Analysis of a 6S glycerol gradient peak of RNA polymerase activity by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of five polypeptides, of molecular weights 72,000, 65,000, 57,000, 45,000, and 35,000. The molecular weights of four of the polypeptides (72,000, 65,000, 45,000, and 35,000) are almost identical to the reported molecular weights of the four subunits of Qβ replicase.

Keywords: BHK 21 cells, smooth membranes, electron microscopy

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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