The treatment of vesicular stomatitis virus with 1% saponin induced the release of envelopes from inner virus structures. The density of treated virus particles in CsCl increased from 1.22 to 1.23 g/ml, probably owing to loss of lipids. The envelopes could be removed from the nucleoprotein helix and further purified by repeatedly ultracentrifuging in sucrose gradients. The haemagglutinating activity of the envelopes was retained. The purified envelopes had sedimentation coefficients of 380 to 400S and a density of 1.20 g/ml. Two proteins, glycoprotein G and large protein L, were dominant in polyacrylamide gel electrophoresis of purified envelopes. In electron microscopy small amounts of ribonucleoprotein N were also seen as free, unwound ribbons, close to the envelopes.


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