Reticulocyte Protein Synthesis: Response of Ribosome Fractions to Polyuridylic Acid
- 19 April 1963
- journal article
- research article
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 140 (3564), 314-316
- https://doi.org/10.1126/science.140.3564.314
Abstract
Reticulocyte ribosomes with sedimentation coefficients greater than 100S ("heavy" ribosomes) appear to be considerably more active in hemoglobin synthesis than are 78S ribosomes. When assayed for the ability to synthesize polyphenylalanine in the presence of polyuridylic acid, the 78S ribosomes and "heavy" ribosomes have similar activities. Polyuridylic acid inhibits incorporation by "heavy" ribosomes of amino acids other than phenylalanine.Keywords
This publication has 12 references indexed in Scilit:
- Polypeptide synthesis in Escherichia coli: II. The polypeptide chain and S-RNAJournal of Molecular Biology, 1963
- Polypeptide synthesis in Escherichia coli: I. ribosomes and the active complexJournal of Molecular Biology, 1963
- Electron Microscope Studies of Ribosomal Clusters Synthesizing HemoglobinScience, 1962
- Fate of a Synthetic Polynucleotide Directing Cell-Free Protein Synthesis II. Association with RibosomesScience, 1962
- Unstable ribonucleic acid in mammalian blood cellsBiochemical and Biophysical Research Communications, 1962
- Function of Polyuridylic Acid and Ribonucleic Acid in Protein Biosynthesis by Ribosomes from Mammalian ReticulocytesNature, 1962
- MESSENGER-RNA ATTACHMENT TO ACTIVE RIBOSOMESProceedings of the National Academy of Sciences, 1962
- Molecular and Biological Characterization of Messenger RNACold Spring Harbor Symposia on Quantitative Biology, 1961
- AMINO ACID INCORPORATION INTO PROTEINS BY ESCHERICHIA COLI RIBOSOMESProceedings of the National Academy of Sciences, 1960
- INCORPORATION IN VITRO OF LABELED AMINO ACIDS INTO PROTEINS OF RABBIT RETICULOCYTESJournal of Biological Chemistry, 1952