Bernabeu C, Vázquez D, Ballesta J P
Eur J Biochem. 1977 Oct 3;79(2):469-72. doi: 10.1111/j.1432-1033.1977.tb11829.x.
Radioactive ribosomes from Escherichia coli were treated with increasing concentrations of NH4Cl in the presence of 50% ethanol. The resulting particles were tested for peptidyl transferase activity as well as for the binding of (U)C-A-C-C-A-Leu-Ac, (U)C-A-C-C-A-Leu, chloramphenicol, lincomycin and erythromycin. At the same time the proteins present in the particles were quantitatively estimated and the amount of each related to the residual activity displayed by the treated ribosomes. It was found that the loss of protein L16 closely paralleled the inactivation of the particles implying an important role for this protein in the structure of the peptidyl transferase center.
在50%乙醇存在的情况下,用浓度不断增加的氯化铵处理来自大肠杆菌的放射性核糖体。对所得颗粒进行肽基转移酶活性测试,以及对(U)C-A-C-C-A-Leu-Ac、(U)C-A-C-C-A-Leu、氯霉素、林可霉素和红霉素的结合测试。同时,对颗粒中存在的蛋白质进行定量估计,并将每种蛋白质的量与经处理的核糖体所显示的残余活性相关联。结果发现,蛋白质L16的损失与颗粒的失活密切平行,这意味着该蛋白质在肽基转移酶中心的结构中起重要作用。