Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system.
Open Access
- 1 January 1966
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 55 (1) , 212-219
- https://doi.org/10.1073/pnas.55.1.212
Abstract
An improved method for the purification of 2 factors (T and G) which are essential for amino-acid polymerization, is described. The T-1 factor is similar to the A-fraction of Allende et al. The G-l factor coincides with the ribosome-linked guanosine triphosphate (GTP)ase, and resembles the previously separated B-fraction except that it is stable in contrast to B. Mainly due to the purification of G, the unrelated GTP hydrolysis could be reduced so that an excess of phosphate release could be observed (apparently dependent on and equivalent to peptide synthesis). One mole of GTP is probably split for every peptide bond formed.This publication has 16 references indexed in Scilit:
- Direction of Reading of the Genetic MessageJournal of Biological Chemistry, 1965
- CHARACTERIZATION OF A RIBOSOME-LINKED GUANOSINE TRIPHOSPHATASE IN ESCHERICHIA COLI EXTRACTSProceedings of the National Academy of Sciences, 1964
- RNA Codewords and Protein SynthesisScience, 1964
- RESOLUTION OF THE E. COLI AMINO ACYL sRNA TRANSFER FACTOR INTO TWO COMPLEMENTARY FRACTIONSProceedings of the National Academy of Sciences, 1964
- SYNTHETIC POLYNUCLEOTIDES AND THE AMINO ACID CODE, VIIProceedings of the National Academy of Sciences, 1962
- Protein synthesis from aminoacyl-soluble ribonucleic acid.1962
- CHARACTERISTICS AND STABILIZATION OF DNAASE-SENSITIVE PROTEIN SYNTHESIS IN E. COLI EXTRACTSProceedings of the National Academy of Sciences, 1961
- EXPERIMENTS ON HEMOGLOBIN BIOSYNTHESISProceedings of the National Academy of Sciences, 1961
- THE EFFECT OF GUANOSINE DIPHOSPHATE AND TRIPHOSPHATE ON THE INCORPORATION OF LABELED AMINO ACIDS INTO PROTEINSJournal of Biological Chemistry, 1956
- PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENTJournal of Biological Chemistry, 1951