| Literature DB >> 824460 |
I Ulmanen, H Söderlund, L Kääriäinen.
Abstract
Semlike forest virus capsid protein cosedimented with the large ribosomal subunit at 60S in sucrose gradients after treatment of cytoplasm from infected cells with Triton X-100 and EDTA. In CsCl gradients the capsid protein banded with the subunit at a density of 1.56 to 1.57 g/cm3. Most of the capsid protein could be detached from the 60S structure by treatment with 0.8 M KCl. The ribonucleoprotein of the 26S RNA had a sedimentation value of 53S and a density of 1.50 g/cm3 and could thus be separated from the 60S structure. The data suggest that the capsid protein binds to the large ribosomal subunit, but not to the viral 26S RNA.Entities:
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Year: 1976 PMID: 824460 PMCID: PMC354981 DOI: 10.1128/JVI.20.1.203-210.1976
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103