Khandjian E W, Türler H
Mol Cell Biol. 1983 Jan;3(1):1-8. doi: 10.1128/mcb.3.1.1-8.1983.
During the lytic infection of monkey and mouse cells with simian virus 40 and polyoma virus, respectively, the preferentially increased synthesis of two host proteins of 92,000 and 72,000 Mr was observed by 15 to 20 h after infection besides the general stimulation of most cellular proteins. The incubation of uninfected monkey and mouse cell cultures for 30 to 60 min at 43.5 degrees C induced the enhanced synthesis of at least three proteins of 92,000, 72,000 and 70,000 Mr, the last one being the major heat shock protein of mammalian cells. Two-dimensional gel electrophoresis and partial proteolytic digestion confirmed that the same 92,000- and 72,000-Mr proteins are stimulated by virus infection and thermal treatment. In simian virus 40-infected CV-1 cells, we also observed the weak stimulation of a 70,000-Mr protein comigrating in gel electrophoresis with the major heat shock protein. The 92,000-, 72,000- and 70,000-Mr proteins of monkey cells are structurally very similar to the corresponding proteins of mouse cells. In immunoprecipitations, no specific association of these proteins to simian virus 40 T antigens was noticed.
在用猿猴病毒40和多瘤病毒分别对猴细胞和小鼠细胞进行裂解感染的过程中，除了大多数细胞蛋白质受到普遍刺激外，在感染后15至20小时观察到两种分子量分别为92,000和72,000的宿主蛋白质的合成优先增加。将未感染的猴细胞和小鼠细胞培养物在43.5摄氏度下孵育30至60分钟，诱导了至少三种分子量分别为92,000、72,000和70,000的蛋白质的合成增加，最后一种是哺乳动物细胞的主要热休克蛋白。二维凝胶电泳和部分蛋白酶解消化证实，病毒感染和热处理刺激的是相同的分子量为92,000和72,000的蛋白质。在猿猴病毒40感染的CV-1细胞中，我们还观察到一种分子量为70,000的蛋白质在凝胶电泳中与主要热休克蛋白共迁移，受到了微弱刺激。猴细胞中分子量为92,000、72,000和70,000的蛋白质在结构上与小鼠细胞的相应蛋白质非常相似。在免疫沉淀中，未发现这些蛋白质与猿猴病毒40 T抗原存在特异性结合。
