The Primary Structure of an Acidic Protein from 50‐S Ribosomes of Escherichia coli which is Involved in GTP Hydrolysis Dependent on Elongation Factors G and T
- 1 April 1973
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 34 (1) , 138-152
- https://doi.org/10.1111/j.1432-1033.1973.tb02740.x
Abstract
No abstract availableKeywords
This publication has 39 references indexed in Scilit:
- Isolation and characterization of two acidic proteins from the 50S subunit required for GTPase activities of both EF G and EF TBiochemical and Biophysical Research Communications, 1972
- Components of the 50S ribosomal subunit involved in GTP cleavageBiochemical and Biophysical Research Communications, 1972
- 50-S Ribsomal Proteins. Peptide Studies on Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coliEuropean Journal of Biochemistry, 1972
- 50-S Ribosomal Proteins. Purification and Partial Characterization of Two Acidic Proteins, A1 and A2, Isolated from 50-S Ribosomes of Escherichia coliEuropean Journal of Biochemistry, 1972
- Ribosomal proteins. XXV. Immunological studies on Escherichia coli ribosomal proteinsJournal of Molecular Biology, 1971
- Ribosomal ProteinsEuropean Journal of Biochemistry, 1971
- Effect of Pregnancy on the Isoantibody Response in RabbitsNature, 1971
- Analysis of the code relating sequence to conformation in proteins: Possible implications for the mechanism of formation of helical regionsJournal of Molecular Biology, 1971
- An isotope dilution procedure for detection and quantitative estimation of phenylthiohydantoins released in the Edman degradationBiochemical and Biophysical Research Communications, 1969
- Human haemoglobin A2Biochimica et Biophysica Acta, 1962