Leader D P, Coia A A
Biochem J. 1978 Nov 15;176(2):569-72. doi: 10.1042/bj1760569.
The acidic ribosomal phosphoprotein, Lgamma, of Krebs II ascites cells was further characterized and compared with proteins L7 and L12 of Escherichia coli. Ribosomal protein Lgamma was selectively removed from 60S sibosomal subunits by 50% ethanol and 1M-NH4Cl, and antibodies raised against protein Lgamma cross-reacted with E. coli protein L12 in immunodiffusion experiments. These and other, previously reported, data support the proposal that the uekaryotic counterpart of E. coli proteins L7 and L12 is phosphorylated.
对克雷布斯II腹水癌细胞的酸性核糖体磷蛋白Lγ进行了进一步表征,并与大肠杆菌的L7和L12蛋白进行了比较。核糖体蛋白Lγ可被50%乙醇和1M氯化铵从60S核糖体亚基中选择性去除,在免疫扩散实验中,针对蛋白Lγ产生的抗体与大肠杆菌蛋白L12发生交叉反应。这些以及之前报道的其他数据支持了这样的提议,即大肠杆菌蛋白L7和L12的真核对应物是磷酸化的。