Ribosomal Proteins

作者：Heide E. Homann, Kund H. Nierhaus · 发表于：European Journal of Biochemistry · 年份：1971 · DOI：10.1111/j.1432-1033.1971.tb01388.x · 被引用次数：154 · 研究领域：RNA and protein synthesis mechanisms、RNA modifications and cancer、RNA Research and Splicing

The 43 S precursor of the 50 S ribosomal subunit shows a protein pattern very similar to that of a “core” particle derived from 50 S subunits on CsCl gradients. A comparison of the protein patterns of “core” particles from 50 S subunits after CsCl equilibration runs or incubation with increasing LiCl concentrations over the molarity range 0.4–6 M revealed that the proteins are successively released from the “core” in five distinct groups. The protein pattern of the 21 S precursor of 30 S ribosomal subunits was compared with that of the reconstituted intermediate particle and LiCl‐treated “core” particles of 30 S subunits. The 21 S is similar to both the reconstituted intermediate and the “core” particles derived by a 1 M LiCl treatment, whereas the reconstituted intermediate and this core particle differ rather more.