<script type="text/javascript">
<!--
document.write('<div id="oa_widget"></div>');
document.write('<script type="text/javascript" src="https://www.openaire.eu/index.php?option=com_openaire&view=widget&format=raw&projectId=undefined&type=result"></script>');
-->
</script>

COPY SCRIPT

For further information contact us at helpdesk@openaire.eu

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

descriptionPublicationkeyboard_double_arrow_right Article 01 Apr 2003 English Publisher:Springer Science and Business Media LLCJournal:Journal of Protein Chemistry, volume 22, pages 249-258 (issn: 0277-8033, eissn: 1573-4943,

Authors: Serguei N. Vladimirov; Galina G. Karpova; Anton V. Ivanov; Brigitte Wittmann-Liebold; Albrecht Otto; Tsezi A. Egorov; Susanne Kostka; +3 Authors

doi: 10.1023/a:1025068419698

pmid: 12962325

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

- Summary
- Subjects
- Related research
  (22)
- Metrics

tips_and_updates
Recommended

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.

Related Organizations

University of Pennsylvania
United States
Russian Academy of Sciences
Russian Federation
Siberian Branch of the Russian Academy of Sciences
Russian Federation
Vavilov Institute of General Genetics
Russian Federation

Keywords

Molecular Weight, Ribosomal Proteins, Sequence Analysis, Protein, Molecular Sequence Data, Humans, Amino Acid Sequence, Protein Processing, Post-Translational, Chromatography, High Pressure Liquid, Mass Spectrometry

22 Research products, page 1 of 3

Homo sapiens
2018IsRelatedTo
60S ribosomal protein L14
2017IsRelatedTo
60S ribosomal protein L18
2017IsRelatedTo
60S ribosomal protein L11
2017IsRelatedTo
60S ribosomal protein L21
2017IsRelatedTo
60S ribosomal protein L10a
2017IsRelatedTo
60S ribosomal protein L17
2017IsRelatedTo
60S ribosomal protein L6
2017IsRelatedTo
60S ribosomal protein L8
2017IsRelatedTo
60S ribosomal protein L35
2017IsRelatedTo

chevron_left
1
2
3
chevron_right

Impact byBIP!

	citations This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	67
	popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.	Top 10%
	influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).	Top 10%
	impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.	Top 10%