Journal of Protein Chemistry

, Volume 22, Issue 3, pp 249–258

Characterization and Analysis of Posttranslational Modifications of the Human Large Cytoplasmic Ribosomal Subunit Proteins by Mass Spectrometry and Edman Sequencing

Authors

  • Tatyana I. Odintsova
    • Russian Academy of SciencesVavilov Institute of General Genetics
    • Protein Chemistry Research GroupMax Delbrueck Center of Molecular Medicine
  • Anton V. Ivanov
    • Siberian Branch of the Russian Academy of SciencesNovosibirsk Institute of Bioorganic Chemistry
  • Tsezi A. Egorov
    • Russian Academy of SciencesShemyakin & Ovchinnikov Institute of Bioorganic Chemistry
  • Ralf Bienert
    • Protein Chemistry Research GroupMax Delbrueck Center of Molecular Medicine
  • Serguei N. Vladimirov
    • Siberian Branch of the Russian Academy of SciencesNovosibirsk Institute of Bioorganic Chemistry
  • Susanne Kostka
    • Protein Chemistry Research GroupMax Delbrueck Center of Molecular Medicine
  • Albrecht Otto
    • Protein Chemistry Research GroupMax Delbrueck Center of Molecular Medicine
    • Chemistry DepartmentUniversity of Pennsylvania
  • Brigitte Wittmann-Liebold
    • Russian Academy of SciencesVavilov Institute of General Genetics
    • WITA GmbH
  • Galina G. Karpova
    • Siberian Branch of the Russian Academy of SciencesNovosibirsk Institute of Bioorganic Chemistry
Article

DOI: 10.1023/A:1025068419698

Cite this article as:
Odintsova, T.I., Müller, E., Ivanov, A.V. et al. J Protein Chem (2003) 22: 249. doi:10.1023/A:1025068419698

Abstract

The 60S ribosomal proteins were isolated from ribosomes of human placenta and separated by reversed phase HPLC. The fractions obtained were subjected to trypsin and Glu-C digestion and analyzed by mass fingerprinting (MALDI-TOF), MS/MS (ESI), and Edman sequencing. Forty-six large subunit proteins were found, 22 of which showed masses in accordance with the SwissProt database (June 2002) masses (proteins L6, L7, L9, L13, L15, L17, L18, L21, L22, L24, L26, L27, L30, L32, L34, L35, L36, L37, L37A, L38, L39, L41). Eleven (proteins L7, L10A, L11, L12, L13A, L23, L23A, L27A, L28, L29, and P0) resulted in mass changes that are consistent with N-terminal loss of methionine, acetylation, internal methylation, or hydroxylation. A loss of methionine without acetylation was found for protein L8 and L17. For nine proteins (L3, L4, L5, L7A, L10, L14, L19, L31, and L40), the molecular masses could not be determined. Proteins P1 and protein L3-like were not identified by the methods applied.

Human ribosomal proteinsmass spectrometryposttranslational modifications

Copyright information

© Plenum Publishing Corporation 2003