Marion M J, Reboud J P
Biochim Biophys Acta. 1981 Jan 29;652(1):193-203. doi: 10.1016/0005-2787(81)90222-7.
Electrophoresis of the 60-S ribosomal subunits from rat liver in the presence of citrate ions removes the 7 S ribonucleoprotein complex between protein L5 and 5 S RNA though this complex is not released by dialysis or by centrifugation through a sucrose cushion in the same buffer. Using acetate instead of citrate, the subunits remain intact in all cases. On the other hand, in the presence of EDTA, the complex is always released. The poly(U) directed polyphenylalanine synthesis is correlated in each case with the presence of this complex within the subunits. The melting curves of subunits which have been treated with citrate, acetate or EDTA and then taken back in the buffer in which they were stored suggest that the specific RNA-protein interactions are preserved in the presence of acetate and of citrate but not of EDTA. As a whole, the results support the interpretation that the association of protein L5 and 5 S RNA exists within the active subunits.
在柠檬酸根离子存在的情况下，对大鼠肝脏的60-S核糖体亚基进行电泳，会去除蛋白质L5和5 S RNA之间的7 S核糖核蛋白复合体，尽管该复合体不能通过透析或在相同缓冲液中通过蔗糖垫层离心而释放。使用醋酸盐代替柠檬酸盐时，在所有情况下亚基都保持完整。另一方面，在EDTA存在的情况下，该复合体总是会被释放。在每种情况下，聚（U）指导的聚苯丙氨酸合成都与该复合体在亚基中的存在相关。用柠檬酸盐、醋酸盐或EDTA处理后再放回储存缓冲液中的亚基的解链曲线表明，在醋酸盐和柠檬酸盐存在时，特定的RNA-蛋白质相互作用得以保留，但在EDTA存在时则不然。总体而言，结果支持这样的解释，即蛋白质L5和5 S RNA的结合存在于活性亚基内。
