Characterization of The Drosophila m elanogaster Ribosomal Proteome
We have combined high-resolution two-dimensional (2-D) gel electrophoresis with mass spectrometry to identifying proteins represented in a 2-D gel database of Drosophila melanogaster ribosomes. First, we purified ribosomes from third instar Drosophila larvae and constructed a high-resolution 2-D gel...
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Veröffentlicht in: | Journal of proteome research 2006-08, Vol.5 (8), p.2025-2032 |
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Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Online-Zugang: | Volltext |
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Zusammenfassung: | We have combined high-resolution two-dimensional (2-D) gel electrophoresis with mass spectrometry to identifying proteins represented in a 2-D gel database of Drosophila melanogaster ribosomes. First, we purified ribosomes from third instar Drosophila larvae and constructed a high-resolution 2-D gel database containing 58 Coomassie blue stained polypeptides. Next, we carried out preparative 2-D PAGE to isolate some of the polypeptides and characterize them by MALDI-TOF. Using this strategy we identified 52 ribosomal spots in the database, and in each case confirmed their identity by MALDI-TOF/TOF. The database can be used to analyze Minute mutants of Drosophila. Keywords: Drosophila • ribosome • proteomics • 2D gels • MALDI-TOF |
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ISSN: | 1535-3893 1535-3907 |
DOI: | 10.1021/pr0601483 |