- Isotope-based analysis of modified tRNA nucleosides correlates modification density with translational efficiency.
Isotope-based analysis of modified tRNA nucleosides correlates modification density with translational efficiency.
Angewandte Chemie (International ed. in English) (2012-10-06)
Caterina Brandmayr, Mirko Wagner, Tobias Brückl, Daniel Globisch, David Pearson, Andrea Christa Kneuttinger, Veronika Reiter, Antje Hienzsch, Susanne Koch, Ines Thoma, Peter Thumbs, Stylianos Michalakis, Markus Müller, Martin Biel, Thomas Carell
PMID23037940
ABSTRACT
Useful diversity: Quantification of modified tRNA nucleobases in different murine and porcine tissues reveals a tissue-specific overall modification content. The modification content correlates with rates of protein synthesis in vitro, suggesting a direct link between tRNA modification levels and tissue-specific translational efficiency.
MATERIALS
Product Number
Brand
Product Description
Sigma-Aldrich
Ribonuclease B from bovine pancreas, BioReagent, ≥50 Kunitz units/mg protein, ≥80% (SDS-PAGE)
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type III-A, ≥85% RNase A basis (SDS-PAGE), 85-140 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type II-A, ≥60% (SDS-PAGE), >= 60 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A from bovine pancreas, (Solution of 50% glycerol, 10mM Tris-HCL pH 8.0)
Sigma-Aldrich
Ribonuclease A from bovine pancreas, for molecular biology, ≥70 Kunitz units/mg protein, lyophilized
Sigma-Aldrich
Ribonuclease A from bovine pancreas, Type X-A, ≥90% (SDS-PAGE), ≥70 Kunitz units/mg protein
Sigma-Aldrich
Ribonuclease A-agarose, ammonium sulfate suspension, 400-1,000 units/g agarose (One ml gel will yield 12-30 units)