Structural analysis of a highly acetylated protein using a curved-field reflectron mass spectrometer.
Structural analysis of a highly acetylated protein using a curved-field reflectron mass spectrometer.
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使用曲场反射质谱仪对高度乙酰化的蛋白质进行结构分析。
DOI：
10.1002/pmic.200401167
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Cotter,RobertJ
中科院分区：
文献类型：
--
作者：
Wang,Dongxia;Thompson,Paul;Cole,PhilipA;Cotter,RobertJ
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.
