Trudel M, Ravaoarinoro M, Payment P
Can J Microbiol. 1980 Aug;26(8):899-904. doi: 10.1139/m80-156.
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 than 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.
风疹病毒的血凝素在用吐温80-乙醚破坏纯化病毒后，通过蔗糖密度梯度差速离心进行纯化。然后将纯化的分离血凝素吸附到脂质体上，该脂质体是通过将卵磷脂和磷酸二鲸蜡酯按3.5:1的摩尔比混合制备的。吸附在病毒体上的血凝素复合物具有更高的沉降速率，从而能够将其与游离血凝素分离。因此，通过在含有0.5M氯化钠的蔗糖密度梯度中进行速率区带离心，可以获得纯净的病毒体制剂。免疫电子显微镜显示这些病毒体与风疹免疫抗血清聚集；这表明血凝素亚基的取向与整个病毒上的取向相同。
