Murphy J F, Rhoads R E, Hunt A G, Shaw J G
Department of Plant Pathology, University of Kentucky, Lexington 40546.
Virology. 1990 Sep;178(1):285-8. doi: 10.1016/0042-6822(90)90405-g.
Preparations of tobacco etch virus (TEV) RNA which were purified by sucrose gradient centrifugation, digested with RNase, and analyzed by SDS-polyacrylamide gel electrophoresis contained proteins of 49, 32, and 24 kDa. The 49- and 24-kDa proteins reacted with polyclonal antiserum to the TEV 49-kDa proteinase while the 32-kDa protein reacted with anti-TEV serum. Further purification of the RNA by centrifugation through CsCl removed the coat protein (32 kDa), but not the 49- and 24-kDa proteins. The 49- and 24-kDa proteins did not migrate into a polyacrylamdie gel when the RNA was not digested with RNase. These results indicate that the VPg of TEV is either the 49-kDa proteinase or the 24 kDa that represents the amino-terminal half thereof.
通过蔗糖梯度离心纯化、用核糖核酸酶消化并用十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分析的烟草蚀纹病毒（TEV）RNA制剂含有49、32和24千道尔顿的蛋白质。49千道尔顿和24千道尔顿的蛋白质与针对TEV 49千道尔顿蛋白酶的多克隆抗血清发生反应，而32千道尔顿的蛋白质与抗TEV血清发生反应。通过氯化铯离心进一步纯化RNA可去除外壳蛋白（32千道尔顿），但不能去除49千道尔顿和24千道尔顿的蛋白质。当RNA不用核糖核酸酶消化时，49千道尔顿和24千道尔顿的蛋白质不会迁移到聚丙烯酰胺凝胶中。这些结果表明，TEV的VPg要么是49千道尔顿的蛋白酶，要么是代表其氨基末端一半的24千道尔顿的蛋白质。
