- 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
RESUMEN
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.
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Ribonucleasa A from bovine pancreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein
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Ribonucleasa A from bovine pancreas, for molecular biology, ≥70 Kunitz units/mg protein, lyophilized
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Ribonucleasa A from bovine pancreas, Type III-A, ≥85% RNase A basis (SDS-PAGE), 85-140 Kunitz units/mg protein
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Ribonucleasa A from bovine pancreas, (Solution of 50% glycerol, 10mM Tris-HCL pH 8.0)
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Ribonucleasa A from bovine pancreas, Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein
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Ribonucleasa A from bovine pancreas, Type II-A, ≥60% (SDS-PAGE), >= 60 Kunitz units/mg protein
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Ribonuclease B from bovine pancreas, BioReagent, ≥50 Kunitz units/mg protein, ≥80% (SDS-PAGE)
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Ribonucleasa A from bovine pancreas, Type X-A, ≥90% (SDS-PAGE), ≥70 Kunitz units/mg protein
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Ribonuclease A-agarose, ammonium sulfate suspension, 400-1,000 units/g agarose (One ml gel will yield 12-30 units)