Bioscience Reports · 1986 · 14 citations · 10 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein BiochemistryProtein-protein InteractionsEnzyme InhibitionNucleic Acid CleavageProtein StructureRibosome FunctionRibonuclease ChemistryRibonuclease MechanismsRibonucleoside ChemistryRibonucleotide ChemistryRibosomal Rna-protein Interactions
Alpha-sarcin and gelonin, two proteins which inactivate the 60S ribosomal subunit, interact with Cibacron blue and bind to blue dextran-Sepharose, from which they are partially desorbed by nucleoside triphosphates and, more efficiently, by homopolynucleotides. It is further shown that the two proteins bind to poly(U)-Sepharose and that homopolynucleotides protect dilute solutions of both inhibitors from inactivation. It is suggested that the presence of a polynucleotide site on alpha-sarcin is related to its ribonuclease activity. The existence of a similar site on gelonin might be a clue to its yet unknown mechanism of action.
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Yaeta Endo, Paul W. Huber, Ira G. Wool · Journal of Biological Chemistry · 1983 · 183 citations · Full text