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Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing

Item Type:Article
Title:Characterization and analysis of posttranslational modifications of the human large cytoplasmic ribosomal subunit proteins by mass spectrometry and Edman sequencing
Creators Name:Odintsova, T.I. and Mueller, E.C. and Ivanov, A.V. and Egorov, T.A. and Bienert, R. and Vladimirov, S.N. and Kostka, S. and Otto, A. and Wittmann-Liebold, B. and Karpova, G.G.
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 PO) 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.
Keywords:Human Ribosomal Proteins, Mass Spectrometry, Posttranslational Modifications
Source:Journal of Protein Chemistry
ISSN:0277-8033
Publisher:Kluwer (U.S.A.)
Volume:22
Number:3
Page Range:249-258
Date:April 2003
Official Publication:https://doi.org/10.1023/A:1025068419698
PubMed:View item in PubMed

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