Autor: |
Eliuk SM; Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158-2517, USA., Maltby D, Panning B, Burlingame AL |
Jazyk: |
angličtina |
Zdroj: |
Molecular & cellular proteomics : MCP [Mol Cell Proteomics] 2010 May; Vol. 9 (5), pp. 824-37. Date of Electronic Publication: 2010 Feb 04. |
DOI: |
10.1074/mcp.M900569-MCP200 |
Abstrakt: |
Epigenetic regulation of chromatin is dependent on both the histone protein isoforms and state of their post-translational modifications. The assignment of all post-translational modification sites for each individual intact protein isoform remains an experimental challenge. We present an on-line reversed phase LC tandem mass spectrometry approach for the separation of intact, unfractionated histones and a high resolution mass analyzer, the Orbitrap, with electron transfer dissociation capabilities to detect and record accurate mass values for the molecular and fragment ions observed. From a single LC-electron transfer dissociation run, this strategy permits the identification of the most abundant intact proteins, determination of the isoforms present, and the localization of post-translational modifications. |
Databáze: |
MEDLINE |
Externí odkaz: |
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