Wiche G, Furtner R, Steinhaus N, Cole R D
J Virol. 1979 Oct;32(1):47-51. doi: 10.1128/JVI.32.1.47-51.1979.
The stability of tubulins present in crude extracts of untransformed BALB/c-3T3 mouse fibroblasts, Chinese hamster lung cells, and various of their simian virus 40 transformants was assessed by measurement of their individual colchicine-binding decay rates. In all cases studied the decays followed the kinetics of first-order reactions, and rates were reduced at low temperatures and by vinblastine sulfate. Under all assay conditions, including different temperatures and protein concentrations, tubulins of normal cells decayed considerably faster than those of simian virus 40-transformed cells. Experiments performed with a number of Chinese hamster lung cell clones transformed with temperature-sensitive simian virus 40 gene A mutants showed a clear correlation between increased tubulin stability and the expression of gene A function. These results suggest that it is T-antigen, the viral gene A product, that affects tubulin.
通过测量未转化的BALB/c-3T3小鼠成纤维细胞、中国仓鼠肺细胞及其各种猿猴病毒40转化体的粗提物中微管蛋白的秋水仙碱结合衰减率，评估了微管蛋白的稳定性。在所有研究的情况下，衰减均遵循一级反应动力学，并且在低温和硫酸长春碱作用下速率降低。在所有测定条件下，包括不同温度和蛋白质浓度，正常细胞的微管蛋白衰减速度比猿猴病毒40转化细胞的微管蛋白衰减速度快得多。用一些经温度敏感的猿猴病毒40基因A突变体转化的中国仓鼠肺细胞克隆进行的实验表明，微管蛋白稳定性增加与基因A功能的表达之间存在明显的相关性。这些结果表明，影响微管蛋白的是病毒基因A产物T抗原。
