- 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
ZUSAMMENFASSUNG
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.
MATERIALIEN
Produktnummer
Marke
Produktbeschreibung
Sigma-Aldrich
Ribonuklease A aus Rinderpankreas, Type I-A, powder, ≥60% RNase A basis (SDS-PAGE), ≥50 Kunitz units/mg protein
Sigma-Aldrich
Ribonuklease A aus Rinderpankreas, for molecular biology, ≥70 Kunitz units/mg protein, lyophilized
Sigma-Aldrich
Ribonuklease A aus Rinderpankreas, Type III-A, ≥85% RNase A basis (SDS-PAGE), 85-140 Kunitz units/mg protein
Sigma-Aldrich
Ribonuklease A aus Rinderpankreas, (Solution of 50% glycerol, 10mM Tris-HCL pH 8.0)
Sigma-Aldrich
Ribonuklease A aus Rinderpankreas, Type XII-A, ≥90% (SDS-PAGE), 75-125 Kunitz units/mg protein
Sigma-Aldrich
Ribonuklease A aus Rinderpankreas, Type II-A, ≥60% (SDS-PAGE), >= 60 Kunitz units/mg protein
Sigma-Aldrich
Ribonuklease B aus Rinderpankreas, BioReagent, ≥50 Kunitz units/mg protein, ≥80% (SDS-PAGE)
Sigma-Aldrich
Ribonuklease A aus Rinderpankreas, 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)