1. Application of CE-MS for the analysis of histones and histone modifications.
- Author
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Faserl, Klaus, Sarg, Bettina, and Lindner, Herbert H.
- Subjects
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HISTONES , *POST-translational modification , *T cell receptors , *STRUCTURAL isomers , *FLOW separation , *CAPILLARY electrophoresis , *EPIGENOMICS , *MASS spectrometry - Abstract
• Highly suitable for the separation of differentially modified intact proteins. • CE-MS enables the analysis of short and hydrophilic peptides. • Sample consumption is in the nanoliter range. • CE-MS enables separation of positional isomers of modified peptides. The analysis, identification and quantification of histones and their post-translational modifications plays a central role in chromatin research and in studying epigenetic regulations during physiological processes. In the last decade analytical strategies based on mass spectrometry have been greatly improved for providing a global view of single modification abundances or to determine combinatorial patterns of modifications. Presented here is a newly developed strategy for histone protein analysis and a number of applications are illustrated with an emphasis on PTM characterization. Capillary electrophoresis is coupled to mass spectrometry (CE-MS) and has proven to be a very promising concept as it enables to study intact histones (top-down proteomics) as well as the analysis of enzymatically digested proteins (bottom-up proteomics). This technology combines highly efficient low-flow CE separations with ionization in a single device and offers an orthogonal separation principle to conventional LC-MS analysis, thus expanding the existing analytical repertoire in a perfect manner. [ABSTRACT FROM AUTHOR]
- Published
- 2020
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