Guérin M F, Hayes D H, Nierhaus K H
Biochimie. 1981 Aug-Sep;63(8-9):699-707. doi: 10.1016/s0300-9084(81)80218-0.
Sedimentation of E. coli 50S ribosomal subunits through sucrose gradients containing 10 mM Mg2+ and high concentrations of NaCl (0.1-1.0 M) leads to removal of proteins L16 and L25. Analyses of the structural and functional properties of the protein depleted particles shows that removal of L16 and L25 from the 50S subunit causes loss of its ability to bind tRNA, to associate with the 30S subunit and to catalyze peptide bond formation. Reassociation of both L16 and L25 with core particles lacking these proteins is necessary for recovery of peptidyl transferase activity.
大肠杆菌50S核糖体亚基在含有10 mM Mg2+和高浓度NaCl（0.1 - 1.0 M）的蔗糖梯度中沉降，会导致蛋白质L16和L25的去除。对蛋白质缺失颗粒的结构和功能特性分析表明，从50S亚基中去除L16和L25会导致其失去结合tRNA、与30S亚基结合以及催化肽键形成的能力。L16和L25与缺乏这些蛋白质的核心颗粒重新结合，对于肽基转移酶活性的恢复是必要的。
