Hsu C H, Kingsbury D W
J Virol. 1982 Apr;42(1):342-5. doi: 10.1128/JVI.42.1.342-345.1982.
The NS protein of vesicular stomatitis virus is the only phosphorylated nucleocapsid protein. The amount of NS phosphorylation appears to regulate the activity of the protein in the transcription of the virus genome. Several methods have been used to separate NS subspecies containing different amounts of phosphate, but the relationships among the subspecies separated by different workers have been unclear. We report that the isoelectric points of NS molecules were abnormally acidic in some commercial ampholytes, but favorable ampholytes resolved multiple phosphorylated NS subspecies with isoelectric points ranging from pH 6.8 to 7.2. The most highly phosphorylated NS molecules had more acidic isoelectric points, and they exhibited greater electrophoretic mobilities in two previously employed electrophoretic systems.
水泡性口炎病毒的NS蛋白是唯一被磷酸化的核衣壳蛋白。NS蛋白的磷酸化程度似乎在调节该蛋白在病毒基因组转录中的活性。已有多种方法用于分离含不同磷酸量的NS亚类，但不同研究者分离出的亚类之间的关系尚不清楚。我们报告称，在某些商业两性电解质中，NS分子的等电点呈异常酸性，但合适的两性电解质可分离出多个磷酸化NS亚类，其等电点范围为pH 6.8至7.2。磷酸化程度最高的NS分子具有更酸性的等电点，并且它们在之前使用的两种电泳系统中表现出更大的电泳迁移率。
