Purification and characterization of peptide-elongation factor 2 (aEF-2) from an extremely halophilic archaebacterium Halobacterium halobium
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1988.tb13727.x/fullpdf
Reference26 articles.
1. A highly efficient poly(U)-dependent poly(Phe) synthesis system for the extreme halophile archaebacterium Halobacterium halobium
2. Differential features of ribosomes and of poly(U)-programmed cell-free systems derived from sulphur-dependent archaebacterial species
3. Testing an alternative model for the ribosomal peptide elongation cycle.
4. Allosteric interactions between the ribosomal transfer RNA-binding sites A and E.
5. Evidence that the three-site model for the ribosomal elongation cycle is also valid in the archaebacterium Halobacterium halobium
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2. Introduction of Additional Charges as an Aid in Protein Purification: Isolation of Elongation Factor 2 from Sulfolobus acidocaldarius by Preparative Isoelectric Focusing Before and After ADP-Ribosylation;Protein Expression and Purification;1994-12
3. Molecular, functional and structural properties of an archaebacterial elongation factor 2;Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression;1992-09
4. Properties of the elongation factor 1alpha in the thermoacidophilic archaebacterium Sulfolobus solfataricus;European Journal of Biochemistry;1991-08
5. Purification and characterization of elongation factor G from bovine liver mitochondria.;Journal of Biological Chemistry;1990-12
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