Signature Ions in MS/MS Spectra for Dansyl-Aminohexyl-QQIV Adducts on Lysine

Autor:	Lawrence M. Schopfer, Oksana Lockridge
Jazyk:	angličtina
Rok vydání:	2020
Předmět:	mass spectrometry Protein Prospector transglutaminase dansylQQIV butyrylcholinesterase plasma proteins Organic chemistry QD241-441
Zdroj:	Molecules, Vol 25, Iss 11, p 2659 (2020)
Druh dokumentu:	article
ISSN:	1420-3049
DOI:	10.3390/molecules25112659
Popis:	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.
Databáze:	Directory of Open Access Journals
Externí odkaz:	https://doaj.org/article/6290ada5a55842ac893d4bbd2b28b64a Zobrazit plný text záznamu View record in DOAJ Plný text ve formátu PDF Plný text ve formátu HTML
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