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 cleavage 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.
journal_name
Proteomicsjournal_title
Proteomicsauthors
Wang D,Thompson P,Cole PA,Cotter RJdoi
10.1002/pmic.200401167subject
Has Abstractpub_date
2005-06-01 00:00:00pages
2288-96issue
9eissn
1615-9853issn
1615-9861journal_volume
5pub_type
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