Finkel T, Der C J, Cooper G M
Cell. 1984 May;37(1):151-8. doi: 10.1016/0092-8674(84)90310-6.
A comparison of proteins encoded by normal human ras genes and by mutant rasH or rasK genes activated in human carcinomas revealed no changes in subcellular localization, posttranslational modification, or guanine nucleotide binding associated with activation. Subcellular fractionation indicated that both normal and activated ras proteins were associated exclusively with the membrane fraction. Furthermore, both normal and activated ras proteins exhibited similar degrees of posttranslational acylation. The KD for dGTP binding was 1.0-2.2 X 10(-8) M, with no consistent differences between normal and activated ras proteins. In addition, a survey of 13 possible competing nucleotides revealed no differences in the specificity of nucleotide binding associated with ras gene activation. These results indicate that structural mutations which activate ras gene transforming activity do not alter the protein's known biochemical parameters and in particular do not affect the protein's intrinsic ability to bind guanine nucleotides.
对正常人类ras基因编码的蛋白质与在人类癌症中被激活的突变型rasH或rasK基因编码的蛋白质进行比较，结果显示，与激活相关的亚细胞定位、翻译后修饰或鸟嘌呤核苷酸结合均未发生变化。亚细胞分级分离表明，正常和激活的ras蛋白都仅与膜组分相关。此外，正常和激活的ras蛋白都表现出相似程度的翻译后酰化。dGTP结合的解离常数（KD）为1.0 - 2.2×10⁻⁸ M，正常和激活的ras蛋白之间没有一致的差异。此外，对13种可能的竞争性核苷酸的调查显示，与ras基因激活相关的核苷酸结合特异性没有差异。这些结果表明，激活ras基因转化活性的结构突变不会改变蛋白质已知的生化参数，尤其不会影响蛋白质结合鸟嘌呤核苷酸的内在能力。
