ISOLATION AND PURIFICATION OF A POLYMERIC FORM OF GLYCOPROTEIN OF RABIES VIRUS
ISOLATION AND PURIFICATION OF A POLYMERIC FORM OF GLYCOPROTEIN OF RABIES VIRUS
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DOI：
10.1099/0022-1317-40-1-131
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发表时间：
1978-01-01
影响因子：
3.8
通讯作者：
KOPROWSKI, H
中科院分区：
文献类型：
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作者：
DIETZSCHOLD, B;COX, JH;KOPROWSKI, H
在与狂犬病病毒膜相关的 3 种主要蛋白质中，只有糖蛋白位于病毒膜的外表面。用 Triton X-100 处理狂犬病病毒并通过等电聚焦纯化制备的糖蛋白在大小和等电点方面是均质的。这种不含磷脂的材料能够在疫苗接种实验中（小鼠）防止狂犬病病毒的致命攻击感染。在非变性条件下分离的该组分的表观分子量约为 400,000。通过 SDS 聚丙烯酰胺凝胶电泳 (PAGE) 分析的相同材料仅由 G 蛋白的多肽链 (MW 80,000) 组成。通过 Triton X-100 释放材料的 PAGE 检测到的次要糖蛋白 (gp 50) 似乎是 G 蛋白的分解产物。因此，去污剂释放的物质代表G蛋白的均聚物。讨论了抗原决定簇是否存在于单体亚基上或者是G蛋白聚合形式的特性。
Of the 3 major proteins associated with the rabies virus membrane, only the glycoprotein was located on the external surface of the virus membrane. Glycoprotein prepared by treatment of rabies virus with Triton X-100 and purified by isoelectric focusing was homogeneuos with respect to size and isoelectric point. This material, which is free of phospholipids, is able to protect in vaccination experiments [in mice] against a lethal challenge infection with rabies virus. The apparent MW of this component isolated under non-denaturing conditions is approximately 400,000. The same material analyzed by SDS polyacrylamide gel electrophoresis (PAGE) consisted soley of polypeptide chains of the G protein (MW 80,000). A minor glycoprotein (gp 50), detected by PAGE of the Triton X-100 released material, appeared to be a breakdown product of the G-protein. Therefore the detergent released material represents homopolymers of the G-protein. Whether the antigenic determinants reside on the monomeric subuint or are a property of the polymeric form of the G-protein is disucssed.