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Application of CE-MS for the analysis of histones and histone modifications.
- Source :
-
Methods . Dec2020, Vol. 184, p125-134. 10p. - Publication Year :
- 2020
-
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]
Details
- Language :
- English
- ISSN :
- 10462023
- Volume :
- 184
- Database :
- Academic Search Index
- Journal :
- Methods
- Publication Type :
- Academic Journal
- Accession number :
- 147407194
- Full Text :
- https://doi.org/10.1016/j.ymeth.2020.01.017