Ultrastructural localization of L and NS enzyme subunits on vesicular stomatitis virus RNPs using gold sphere-staphylococcal protein A-monospecific IgG conjugates.
Ultrastructural localization of L and NS enzyme subunits on vesicular stomatitis virus RNPs using gold sphere-staphylococcal protein A-monospecific IgG conjugates.
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DOI：
10.1016/0042-6822(85)90348-4
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发表时间：
1985-04
期刊：
影响因子：
3.7
通讯作者：
S. Harmon;E. Robinson;D. Summers
中科院分区：
文献类型：
--
作者：
S. Harmon;E. Robinson;D. Summers
胶体金球涂有葡萄球菌蛋白A，并使用单特异性抗NS和抗L IgG制剂来确定NS和L蛋白在水泡性口炎病毒（VSV）核糖核蛋白（RNP）复合物上的位置。使用抗NS或抗L的缀合物证明这些酶亚基沿RNP复合物的整个长度均匀分布沿着。在IgG浓度饱和条件下，观察到每个RNP复合物至少有60-70个NS蛋白分子和30-35个L蛋白分子被标记。
Colloidal gold spheres were coated with staphylococcal protein A and were used to determine the location of NS and L proteins on vesicular stomatitis virus (VSV) ribonucleoprotein (RNP) complexes using monospecific anti-NS and anti-L IgG preparations. Conjugates using either anti-NS or anti-L demonstrated that these enzyme subunits were uniformly distributed along the entire length of the RNP complex. Under saturating conditions of IgG concentrations, it was observed that there were at least 60–70 molecules of NS protein and 30–35 molecules of L protein labeled per RNP complex.