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Evaluation of glycosylation site heterogeneity and selective identification of glycopeptides in proteolytic digests of bovine α 1 ‐acid glycoprotein by mass spectrometry
Author(s) -
Hunter Ann P.,
Games David E.
Publication year - 1995
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.1290090111
Subject(s) - chemistry , chromatography , glycopeptide , mass spectrometry , glycoprotein , glycosylation , electrospray , tandem mass spectrometry , protein mass spectrometry , sample preparation in mass spectrometry , liquid chromatography–mass spectrometry , capillary electrophoresis , fragmentation (computing) , electrospray ionization , biochemistry , computer science , operating system , antibiotics
Glycosylation sites in bovine α 1 ‐acid glycoprotein (AGP) have been identified, and the inherent heterogeneity evaluated, by capillary electrophoretic and reversed‐phase liquid chromatography/electrospray‐mass spectrometric analyses of proteolytic digests of this glycoprotein. The success of these methods in locating glycopeptides relied on significant heterogeneity within each glycosylation site. In order to rapidly locate sites in glycoproteins of any degree of heterogeneity, a novel mass spectrometric method was applied to selectively identify the glycopeptides in a proteolytic digest of bovine α 1 ‐AGP. The glycopeptides were selectively located by the generation and detection of characteristic oxonium ions from the carbohydrate moieties by collision‐induced dissociation (CID) during liquid chromatography/electrospray‐tandem mass spectrometry, and liquid chromatography/CID mass spectrometry, in which fragmentation was induced in the supersonic expansion region of the electrospray source.