Abstract
Matrix-assisted laser desorption/ionization mass spectrometry and tandem mass spectrometry (MS/MS) were used to determine the multiple acetylation sites in the histone acetyltransferase (HAT): p300-HAT. Partial deavage of the peptides containing acetylated lysine residues by trypsin provided a set of nested sequences that enabled us to determine that multiple acetylation occurs on the same molecule. At the same time, cleavages resulting in a terminal unacetylated lysine suggested that not all of these sites are fully modified. Using MS and MS/MS, we were able to characterize both the unmodified and acetylated tryptic peptides covering more than 82% of the protein.
Original language | English (US) |
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Pages (from-to) | 2288-2296 |
Number of pages | 9 |
Journal | Proteomics |
Volume | 5 |
Issue number | 9 |
DOIs | |
State | Published - Jun 2005 |
Externally published | Yes |
Keywords
- Acetylation
- Amino acid sequencing
- Mass spectrometry
- Matrix-assisted laser desorption/ionization-time of flight
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology