Salt‐stable association of simian virus 40 capsid with simian virus 40 DNA
- 11 February 1985
- journal article
- Published by Wiley in FEBS Letters
- Vol. 181 (1) , 64-68
- https://doi.org/10.1016/0014-5793(85)81114-5
Abstract
In 8 M CsCl, a fraction of the wild-type previrions and tsB228 nucleoprotein complexes lose their core histones but retain their capsid. These histone-depleted complexes apear in the electron microscope as a protein shell attached to supercoiled DNA. Consistent with this result, we find that in l M NaCl, the wildtype previrions dissociate into two populations of nucleoprotein complexes. One population sediments between 50 and 140 S and morphologically resembles the shell-DNA complexes isolated in CsCl gradients. The other population is comprised primarily of nucleoproteins which sediment at 40 S.Keywords
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