Rosato R R, Robbins M L, Eddy G A
J Virol. 1974 Apr;13(4):780-7. doi: 10.1128/JVI.13.4.780-787.1974.
Analysis of purified Oriboca virions by neutral, sodium dodecyl sulfate polyacrylamide-gel electrophoresis indicated the presence of three structural polypeptides designated V-1, V-2, and V-3 on the basis of their relative electrophoretic mobilities in 8% gels. Polypeptides V-2 and V-3 are glycopeptides associated with the virion envelope as demonstrated by the preferential incorporation of labeled glucosamine into the polypeptides and by release of the polypeptides from the intact virion by the nonionic detergent NP-40. Polypeptide V-1 is the protein component of the nucleoprotein core of Oriboca virus as evidenced by the specific incorporation of uridine into the nucleoprotein, its release from the intact virion by NP-40 treatment, and its separation by both rate-zonal and isopycnic density gradient centrifugation from both the intact virion and envelope components. Molecular weights have been tentatively assigned to the polypeptides by extrapolation from the structural polypeptides of Sindbis virus when both are run in the same gel. Polypeptide V-1 has an apparent molecular weight of 20,000 to 23,000; V-2, 30,000 to 32,000; and V-3, 83,000 to 85,000.
通过中性十二烷基硫酸钠聚丙烯酰胺凝胶电泳对纯化的奥里博卡病毒粒子进行分析，结果表明，根据它们在8%凝胶中的相对电泳迁移率，存在三种结构多肽，分别命名为V-1、V-2和V-3。多肽V-2和V-3是与病毒粒子包膜相关的糖肽，这可通过标记的葡糖胺优先掺入多肽以及通过非离子去污剂NP-40从完整病毒粒子中释放多肽得到证明。多肽V-1是奥里博卡病毒核蛋白核心的蛋白质成分，这可通过尿苷特异性掺入核蛋白、经NP-40处理后从完整病毒粒子中释放以及通过速率区带离心和等密度密度梯度离心从完整病毒粒子和包膜成分中分离得到证明。当两种病毒粒子在同一凝胶中进行电泳时，通过从辛德毕斯病毒的结构多肽进行外推，已初步确定了这些多肽的分子量。多肽V-1的表观分子量为20,000至23,000；V-2为30,000至32,000；V-3为83,000至85,000。
