Ulmanen I, Söderlund H, Kääriäinen L
J Virol. 1976 Oct;20(1):203-10. doi: 10.1128/JVI.20.1.203-210.1976.
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.
在用Triton X-100和EDTA处理感染细胞的细胞质后，辛德毕斯病毒衣壳蛋白在蔗糖梯度中与60S的大核糖体亚基一起沉降。在氯化铯梯度中，衣壳蛋白与该亚基一起形成条带，密度为1.56至1.57 g/cm³。通过用0.8 M KCl处理，大多数衣壳蛋白可以从60S结构上分离下来。26S RNA的核糖核蛋白沉降值为53S，密度为1.50 g/cm³，因此可以与60S结构分离。数据表明，衣壳蛋白与大核糖体亚基结合，但不与病毒26S RNA结合。
