Sokol F, Tan K B, McFalls M L, Madore P
J Virol. 1974 Jul;14(1):145-51. doi: 10.1128/JVI.14.1.145-151.1974.
Partial acid hydrolysates of the [(32)P]phosphate- or [(3)H]serine-labeled proteins of purified vesicular stomatitis, rabies, Lagos bat, Mokola, or spring viremia of carp virions and of purified intracellular nucleocapsids of these viruses have been analyzed by paper electrophoresis for the presence of phosphorylated amino acids. Both phosphoserine and phosphothreonine, with the former predominant, were present in virion and nucleocapsid preparations that contained phosphoproteins. An exception was the fish rhabdovirus, which contained only phosphoserine. When vesicular stomatitis or rabies virus proteins were phosphorylated in a cell-free system by the virion-associated protein kinase and analyzed for the presence of phosphorylated amino acid residues, phosphoserine was again found to be more abundant than phosphothreonine. After in vitro protein phosphorylation, another phospho-compound, possibly a third phosphoamino acid, was detected in the partial acid hydrolysates of these viruses.
通过纸电泳分析了纯化的水疱性口炎病毒、狂犬病病毒、拉各斯蝙蝠病毒、莫科拉病毒或鲤鱼春季病毒血症病毒粒子以及这些病毒纯化的细胞内核衣壳中用[³²P]磷酸盐或[³H]丝氨酸标记的蛋白质的部分酸水解产物，以检测磷酸化氨基酸的存在。磷酸丝氨酸和磷酸苏氨酸在含有磷蛋白的病毒粒子和核衣壳制剂中均有存在，前者占主导。唯一的例外是鱼类弹状病毒，它只含有磷酸丝氨酸。当水疱性口炎病毒或狂犬病病毒蛋白在无细胞系统中被病毒粒子相关蛋白激酶磷酸化并分析磷酸化氨基酸残基的存在时，再次发现磷酸丝氨酸比磷酸苏氨酸更丰富。体外蛋白质磷酸化后，在这些病毒的部分酸水解产物中检测到另一种磷化合物，可能是第三种磷酸氨基酸。
