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• W2028396705 abstract "The hemagglutinin of rubella virus has been purified by differential centrifugation through a sucrose density gradient after disruption of purified virus with Tween 80 – ether. The purified isolated hemagglutinin was then adsorbed on liposomes which had been prepared by mixing lecithin and dicetyl phosphate in a 3.5:1 molar ratio. The complex of hemagglutinin adsorbed on the virosomes had a higher sedimentation rate, enabling their separation from free hemagglutinin. It was thus possible to obtain a pure preparation of virosomes by rate zonal centrifugation in a sucrose density gradient containing 0.5 M NaCl. Immunoelectron microscopy showed aggregation of these virosomes with a rubella immune antiserum; this would suggest that the HA subunits are oriented in the same way as on the whole virus." @default.
• W2028396705 created "2016-06-24" @default.
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• W2028396705 date "1980-08-01" @default.
• W2028396705 modified "2023-09-25" @default.
• W2028396705 title "Reconstitution of rubella hemagglutinin on liposomes" @default.
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• W2028396705 doi "https://doi.org/10.1139/m80-156" @default.
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