Identification of human, rat and chicken ribosomal proteins by a combination of two-dimensional polyacrylamide gel electrophoresis and mass spectrometry

Anh Thu Nguyen-Lefebvre, Sandrine Gonin-Giraud, Alexander Scherl, Patrizia Arboit, Laure Granger, Jean Charles Sanchez, Jean Jacques Diaz, Olivier Gandrillon, Jean Jacques Madjar

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

To identify the exact spot position of human, rat and chicken ribosomal proteins (RP) separated by two-dimensional polyacrylamide gel electrophoresis (2-DE), a 2-DE system was designed to separate RP with a pI. >. 8.6 according to their charge in the first dimension and to their molecular mass in the second dimension. Individual proteins were excised from the gels and identified by mass spectrometry after digestion by trypsin. In addition, a mixture of purified RP from these three species was also analyzed by tandem mass tag spectrometry. By combining those two methods 74 RP from human, 76 from rat and 67 from chicken were identified according to the nomenclature initially defined for rat liver RP and by using the Swiss-Prot/trEMBL databases. Whereas human and rat RP were well described, most of RP from chicken were not characterized in databases, since 35 out of 67 chicken RP identified in this study were not listed yet. We propose here the first comprehensive description of chicken RP and their comparison to those from human and rat.

Original languageEnglish (US)
Pages (from-to)167-185
Number of pages19
JournalJournal of Proteomics
Volume74
Issue number2
DOIs
StatePublished - Feb 1 2011
Externally publishedYes

Keywords

  • Chicken
  • Human
  • Mass spectrometry
  • Rat
  • Ribosomal proteins
  • Two-dimensional polyacrylamide gel electrophoresis

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry

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    Nguyen-Lefebvre, A. T., Gonin-Giraud, S., Scherl, A., Arboit, P., Granger, L., Sanchez, J. C., Diaz, J. J., Gandrillon, O., & Madjar, J. J. (2011). Identification of human, rat and chicken ribosomal proteins by a combination of two-dimensional polyacrylamide gel electrophoresis and mass spectrometry. Journal of Proteomics, 74(2), 167-185. https://doi.org/10.1016/j.jprot.2010.10.007