Isolation of a 5S RNA-Protein L5 Complex from 60S Subunits of Rat Liver Ribosomes by Cesium Sulfate Density-Gradient Equilibrium Centrifugation
Autor: | Noboru Isoda, Kiichi Ishikawa, Tatsuo Tanaka |
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Rok vydání: | 1981 |
Předmět: |
Male
Ribosomal Proteins Density gradient Cesium Biology Biochemistry Ribosome Drug Stability Centrifugation Density Gradient Animals Centrifugation Equilibrium Centrifugation Molecular Biology Ribonucleoprotein Eukaryotic Large Ribosomal Subunit Osmolar Concentration RNA Rats Inbred Strains General Medicine Ribosomal RNA Rats Liver Solubility RNA Ribosomal Electrophoresis Polyacrylamide Gel Ribosomes |
Zdroj: | The Journal of Biochemistry. 90:551-554 |
ISSN: | 1756-2651 0021-924X |
DOI: | 10.1093/oxfordjournals.jbchem.a133504 |
Popis: | Upon CS2SO4 density-gradient equilibrium centrifugation, 60S subunits of rat liver ribosomes were dissociated to form three bands at the densities of 1.55, 1.40, and 1.30 g/ml. The bands at 1.55 and 1.30 g/ml were shown to contain exclusively RNA or proteins, respectively, whereas the band at 1.40 g/ml contained both RNA and a protein. The RNA in the 1.40 g/ml band was identified as 5S RNA and the protein in this band was protein L5. An empirical calculation suggested that the 1.40 g/ml band contained an equimolar 5S RNA-protein L5 ribonucleoprotein complex. This finding may indicate that protein L5 is located in very close proximity to 5S RNA in large ribosomal subunits. |
Databáze: | OpenAIRE |
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