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Abstract
Southern bean mosaic virus (SBMV) and sowbane mosaic virus (SoMV) were each dissociated into RNA and protein components in neutral pH buffers containing ethylenediaminetetraacetic acid and 1 M NaCl. The assembly of SBMV particles and of SoMV RNA in SBMV protein was accomplished by dialysis of the virus components into low molarity buffers containing divalent metal ions. Some of these particles were stable in 1% sodium dodecyl sulfate (SDS) and had sedimentation and electrophoretic properties identical with untreated virus. Spherical particles were also assembled with either SBMV or SoMV RNA in SoMV protein and with sodium dextran sulfate in either SBMV or SoMV protein, but these particles were not stable in 1% SDS.
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