Structural analysis of a highly acetylated protein using a curved‐field reflectron mass spectrometer | Zendy

Wang Dongxia | Zendy; Thompson Paul | Zendy; Cole Philip A. | Zendy; Cotter Robert J. | Zendy

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Structural analysis of a highly acetylated protein using a curved‐field reflectron mass spectrometer

Author(s) -

Wang Dongxia,

Thompson Paul,

Cole Philip A.,

Cotter Robert J.

Publication year - 2005

Publication title -

proteomics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.26

H-Index - 167

eISSN - 1615-9861

pISSN - 1615-9853

DOI - 10.1002/pmic.200401167

Subject(s) - acetylation , mass spectrometry , lysine , tandem mass spectrometry , reflectron , chemistry , chromatography , protein mass spectrometry , isobaric labeling , trypsin , sample preparation in mass spectrometry , p300 cbp transcription factors , acetyltransferase , biochemistry , electrospray ionization , organic chemistry , time of flight mass spectrometry , ionization , amino acid , histone acetyltransferases , enzyme , ion , gene

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.

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