Mellon M G, Emerson S U
J Virol. 1978 Sep;27(3):560-7. doi: 10.1128/JVI.27.3.560-567.1978.
The L and NS proteins of vesicular stomatitis virions (New Jersey serotype) were solubilized with Triton X-100 and high-salt buffer and recombined with purified nucleocapsids under conditions similar to those used to reconstitute transcriptase activity in vitro. The nucleocapsid-bound L and NS proteins were separated from unbound proteins on a glycerol gradient. The rebinding of L and NS proteins mimics the in vivo binding in that at saturation the ratio of L and NS molecules to N molecules is approximately the same as observed in the intact virion. L and NS proteins were separated and added back independently and in combination to the template. The purified NS protein bound to the template in the absence of L protein. However, the L protein binding appeared to depend on the presence of NS protein. The presence of Mg2+ and nucleotides, which is required for transcription, was not necessary for the rebinding of L and NS proteins.
水泡性口炎病毒粒子（新泽西血清型）的L蛋白和NS蛋白用 Triton X - 100和高盐缓冲液溶解，并在类似于体外重建转录酶活性所用的条件下与纯化的核衣壳重组。通过甘油梯度将与核衣壳结合的L蛋白和NS蛋白与未结合的蛋白分离。L蛋白和NS蛋白的重新结合模拟了体内结合情况，即在饱和状态下，L分子和NS分子与N分子的比例与完整病毒粒子中观察到的大致相同。L蛋白和NS蛋白被分离出来，并分别或组合添加回模板中。纯化的NS蛋白在没有L蛋白的情况下与模板结合。然而，L蛋白的结合似乎依赖于NS蛋白的存在。转录所需的Mg2+和核苷酸的存在对于L蛋白和NS蛋白的重新结合不是必需的。
