Vainionpää R
Arch Virol. 1979;60(3-4):239-48. doi: 10.1007/BF01317495.
The synthesis of wild-type measles virus-specified polypeptides in Vero cells in pulse-chase experiments, in cells with synchronized protein synthesis by high salt concentration, and in the presence of proteolytic enzyme inhibitors was analyzed by polyacrylamide slab-gel electrophoresis. Six major (L, G, 2, NP, 5 and M) structural polypeptides were identified in infected cells. The results of pulse-chase experiments suggested that most of the structural polypeptides were synthesized at their final length. Polypeptide M was found to be sensitive to trypsin. In TLCK-treated cells its molecular weight was about 1000--2000 daltons higher than in untreated cells. A minor virus-specific polypeptide with a molecular weight of about 23,000 was found as a very faint and diffuse band. In addition, three nonstructural polypeptides with molecular weights of 65,000, 38,000 and 18,000 were also detected. The experiments with proteolytic enzyme inhibitors and with synchronized protein synthesis suggested that the polypeptide with a molecular weight of 65,000 might be a precursor of the structural polypeptide 5.
通过聚丙烯酰胺平板凝胶电泳分析了在脉冲追踪实验中、在高盐浓度同步蛋白质合成的细胞中以及在存在蛋白水解酶抑制剂的情况下，野生型麻疹病毒在Vero细胞中指定多肽的合成情况。在受感染的细胞中鉴定出六种主要的（L、G、2、NP、5和M）结构多肽。脉冲追踪实验的结果表明，大多数结构多肽是以其最终长度合成的。发现多肽M对胰蛋白酶敏感。在经TLCK处理的细胞中，其分子量比未处理的细胞高约1000 - 2000道尔顿。发现一种分子量约为23,000的次要病毒特异性多肽呈现为非常微弱且弥散的条带。此外，还检测到三种分子量分别为65,000、38,000和18,000的非结构多肽。蛋白水解酶抑制剂实验和同步蛋白质合成实验表明，分子量为65,000的多肽可能是结构多肽5的前体。
