Studies on Polypeptide Elongation Factors from Escherichia coli II. PURIFICATION OF FACTORS Tu-GUANOSINE DIPHOSPHATE, Ts, AND Tu-Ts, AND CRYSTALLIZATION OF Tu-GUANOSINE DIPHOSPHATE AND Tu-Ts
TLDR
The polypeptide elongation factors Tu-GDP, Ts and Tu-Ts have been purified from Escherichia coli to homogeneous state as judged by criteria of ultracentrifugation and disc gel electrophoresis.About:
This article is published in Journal of Biological Chemistry.The article was published on 1972-11-10 and is currently open access. It has received 236 citations till now. The article focuses on the topics: Column chromatography & Ammonium sulfate.read more
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G PROTEIN MECHANISMS: Insights from Structural Analysis
TL;DR: This review is concerned with the structures and mechanisms of a superfamily of regulatory GTP hydrolases (G proteins), which include Ras and its close homologs, translation elongation factors, and heterotrimeric G proteins.
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Patterns of predation in a diverse predator-prey system.
TL;DR: Biodiversity allows both predation (top-down) and resource limitation (bottom-up) to act simultaneously to affect herbivore populations.
Journal ArticleDOI
The role of guanosine 5'-triphosphate in polypeptide chain elongation.
Journal ArticleDOI
Isolation and Characterization of the Human Chromosomal Gene for Polypeptide Chain Elongation Factor-1α
TL;DR: By using nuclear extracts from HeLa cells, the promoter of human elongation factor-1 alpha gene could stimulate in vitro transcription better than the adenovirus major late promoter.
Journal ArticleDOI
The structure of the Escherichia coli EF-Tu. EF-Ts complex at 2.5 Å resolution
TL;DR: The crystal structure of the EF- Tu·EF-Ts complex from Escherichia coli has been determined to a resolution of 2.5 Å and the interaction of EF-Ts with EF-Tu results principally in the disruption of the Mg2+ ion binding site, thereby reducing the affinity of EF -Tu for guanine nucleotides.
References
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Book ChapterDOI
[10] Protein fractionation on the basis of solubility in aqueous solutions of salts and organic solvents
Journal ArticleDOI
Studies on the purification and properties of factor Tu from E. coli.
TL;DR: Transfer factor Tu has been purified to apparent homogeneity from extracts of Escherichia coli and contains a sulfhydryl group essential for GDP binding, which in Tu free of nucleotide reacts readily with N-ethylmaleimide, but in Tu-GDP is almost inert.
Journal ArticleDOI
Separation of three microbial amino acid polymerization factors.
Jean Lucas-Lenard,Fritz Lipmann +1 more
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Comparison of guanosine triphosphate split and polypeptide synthesis with a purified E. coli system.
Yasutomi Nishizuka,Fritz Lipmann +1 more
Journal ArticleDOI
Hydrolysis of Guanosine 5'-Triphosphate Associated with Binding of Aminoacyl Transfer Ribonucleic Acid to Ribosomes
TL;DR: It is concluded that, although GTP hydrolysis resulted from the binding of aminoacyl-tRNA to ribosomes in a 1:1 stoichiometry, the two reactions were not tightly coupled under all experimental conditions.