1. MS spectra of intact histones (A) and peptides 1–41 (B) of the second H2A HPLC peak.A, molecular masses of intact histones H2A determined after deconvolution of the multiply charged ion series.
MS spectra of intact histones (A) and peptides 1–41 (B) of the second H2A HPLC peak.A, molecular masses of intact histones H2A determined after deconvolution of the multiply charged ion series. Unmodified, acetylated, and phosphorylated histone H2AC; unmodified and phosphorylated histone H2AE; and histone H2AL, H2AG, H2AA, and Q96KK5 variants were assigned. The dots represent non-attributed molecular masses. B, nano-ESI-MS spectrum of endoproteinase Glu-C peptide 1–41. The ions at m/z , , and were identified as [M + 8H]8+ of unmodified peptide 1–41 from H2AC, H2AE, and Q96KK5; acetylated peptide 1–41 from H2AC; and phosphorylated peptides 1–41 from H2AC and/or H2AE, respectively. The ions at m/z and were characterized as [M + 8H]8+ of peptide 1–41 from H2AL and H2AA and/or H2AG, respectively. The asterisks represent peptides with a different charge state, unrelated to peptide 1–41 of histone H2A. Ac, acetylated; P, phosphorylated.
Débora Bonenfant et al. Mol Cell Proteomics 2006;5:
© 2006 The American Society for Biochemistry and Molecular Biology