Characterization and Analysis of Posttranslational Modifications of the Human Large Cytoplasmic Ribosomal Subunit Proteins by Mass Spectrometry and Edman Sequencing
Copyright policy )Characterization and Analysis of Posttranslational Modifications of the Human Large Cytoplasmic Ribosomal Subunit Proteins by Mass Spectrometry and Edman Sequencing
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.
- Russian Academy of Sciences Russian Federation
- Department of Biological Sciences Russian Federation
- Vavilov Institute of General Genetics Russian Federation
- Siberian Branch of the Russian Academy of Sciences Russian Federation
- University of Pennsylvania United States
Molecular Weight, Ribosomal Proteins, Sequence Analysis, Protein, Molecular Sequence Data, Humans, Amino Acid Sequence, Protein Processing, Post-Translational, Chromatography, High Pressure Liquid, Mass Spectrometry
Molecular Weight, Ribosomal Proteins, Sequence Analysis, Protein, Molecular Sequence Data, Humans, Amino Acid Sequence, Protein Processing, Post-Translational, Chromatography, High Pressure Liquid, Mass Spectrometry
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