Signature Ions in MS/MS Spectra for Dansyl-Aminohexyl-QQIV Adducts on Lysine
Copyright policy )Signature Ions in MS/MS Spectra for Dansyl-Aminohexyl-QQIV Adducts on Lysine
Bacterial transglutaminase was used to label human plasma proteins with fluorescent tags. Protein lysines were modified with dansyl-epsilon-aminohexyl-Gln-Gln-Ile-Val-OH (dansylQQIV), while protein glutamines were modified with dansyl cadaverine. Labeled proteins included human butyrylcholinesterase, apolipoprotein A-1, haptoglobin, haptoglobin-related protein, immunoglobulin heavy chain, and hemopexin. Tryptic peptides were analyzed by LC-MS/MS on an Orbitrap Fusion Lumos mass spectrometer. Modified residues were identified in Protein Prospector and Proteome Discoverer searches of mass spectrometry data. The MS/MS fragmentation spectra from dansylQQIV-modified peptides gave intense peaks at 475.2015, 364.1691, 347.1426, 234.0585, and 170.0965 m/z. These signature ions are useful markers for identifying modified peptides. Human butyrylcholinesterase retained full activity following modification by dansylQQIV or dansyl cadaverine.
Dansyl Compounds, Glutamine, Lysine, Organic chemistry, Article, transglutaminase, dansylQQIV, QD241-441, Tandem Mass Spectrometry, Butyrylcholinesterase, Cadaverine, Protein Prospector, butyrylcholinesterase, Humans, mass spectrometry, plasma proteins
Dansyl Compounds, Glutamine, Lysine, Organic chemistry, Article, transglutaminase, dansylQQIV, QD241-441, Tandem Mass Spectrometry, Butyrylcholinesterase, Cadaverine, Protein Prospector, butyrylcholinesterase, Humans, mass spectrometry, plasma proteins
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