Identification of the tRNA-binding sites on rat liver ribosomes by affinity labeling

@article{Czernilofsky2004IdentificationOT,
  title={Identification of the tRNA-binding sites on rat liver ribosomes by affinity labeling},
  author={A. Czernilofsky and E. Collatz and A. Gressner and I. Wool and E. K{\"u}chler},
  journal={Molecular and General Genetics MGG},
  year={2004},
  volume={153},
  pages={231-235}
}
Summaryp-Nitrophenoxycarbonyl-3H-phenylalanyl-tRNAyeastPhebinds to 80S rat liver ribosomes and forms a covalent bond with ribosomal proteins. The affinity labeled proteins were identified by a kind of “three-dimensional” electrophoresis: groups of 80S proteins were cut out of two-dimensional gel slabs, eluted, and separated by electrophoresis in polyacrylamide gels containing sodium dodecyl sulfate; finally, the radioactivity in the protein bands was determined. The proteins L32/L33, L36, L21… Expand

Figures and Tables from this paper

References

SHOWING 1-10 OF 26 REFERENCES
Proteins at the tRNA binding sites of Escherichia coli ribosomes.
Studies on proteins of animal ribosomes. Affinity labeling of rat liver ribosomes by N‐bromoacetylpuromycin
Identification of a protein at the ribosomal donor-site by affinity labeling.
Peptidyl transferase center of rat-liver ribosome cores.
Studies on proteins of animal ribosomes. XIII. enumeration of ribosomal proteins of rat liver
Affinity label for the tRNA binding site on the Escherichia coli ribosome.
Chemical studies on methionyl-tRNA synthetase from Escherichia coli.
...
1
2
3
...