Analysis of Histone Modifications from Tryptic Peptides of Deuteroacetylated Isoforms.

ABSTRACT: The in vitro deuteroacetylation of histones obtained from biological sources has been used previously in bottom-up mass spectrometry analyses to quantitate the percent of endogenous acetylation of specific lysine sites and/or peptides. In this report, derivatization of unmodified lysine residues on histones is used in combination with high performance mass spectrometry, including combined HPLC MS/MS, to distinguish and quantitate endogenously acetylated isoforms occurring within the same tryptic peptide sequence and to extend this derivatization strategy to other post-translational modifications, specifically methylation, dimethylation and trimethylation. The in vitro deuteroacetylation of monomethylated lysine residues is observed, though dimethylated or trimethylated residues are not der

SUBMITTER: Hersman E 

PROVIDER: S-EPMC3289288 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature