Schreier E, Schweiger B, Stompor S, Stompor B, Schulze P, Michel S
Department of Molecular Biology, Central Institute of Hygiene, Microbiology and Epidemiology, Berlin, G.D.R.
Acta Virol. 1988 Jul;32(4):289-95.
Ribonucleoprotein (RNP) cores were prepared from various strains of human influenza virus by treating the purified or spikeless virus particles with non-ionic detergents such as Nonidet P-40 and centrifugation in continuous linear glycerol gradients. In addition to RNA, the purified complexes contained viral nucleoprotein (NP) and the three P proteins (PA, PB1, PB2) as determined by polyacrylamide gel electrophoresis (PAGE) under denaturing conditions. Contaminations with other viral polypeptides, especially HA1, HA2 and M were below 1%. All RNP complexes were transcriptionally active in vitro. Comparison of the polymerase activity of purified complexes revealed considerable differences depending not only on the content of polymerase proteins. The activity of RNP complexes was enhanced for all strains tested by adding of ApG.
通过用非离子去污剂（如诺乃洗涤剂P-40）处理纯化的或无刺突的病毒颗粒，并在连续线性甘油梯度中离心，从各种人类流感病毒株制备核糖核蛋白（RNP）核心。除RNA外，经变性条件下的聚丙烯酰胺凝胶电泳（PAGE）测定，纯化的复合物还含有病毒核蛋白（NP）和三种P蛋白（PA、PB1、PB2）。其他病毒多肽的污染，尤其是HA1、HA2和M，低于1%。所有RNP复合物在体外均具有转录活性。纯化复合物聚合酶活性的比较显示，不仅取决于聚合酶蛋白的含量，还存在相当大的差异。通过添加ApG，所有测试毒株的RNP复合物活性均增强。
