Characterization of protein glycoforms by capillary zone electrophoresis-nanoelectrospray mass spectrometry

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DOIResolve DOI: http://doi.org/10.1016/S0021-9673(97)00937-0
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TypeArticle
Journal titleJournal of Chromatography A
ISSN0021-9673
Volume794
Issue1-2
Pages327344; # of pages: 18
SubjectMass spectrometry; Glycoproteins; 1-α-Amylase inhibitor; Caseins
AbstractThe investigation of N- and O-linked glycoproteins using capillary-zone electrophoresis interfaced with nanoelectrospray mass spectrometry is described. The combination of high-resolution separation with high-sensitivity mass spectrometric detection provides analysis of glycoprotein digests at sample loadings of high femtomoles to low picomoles. Stepped-orifice voltage scanning is used to identify glycopeptides in complex proteolytic digests. Further structural information is obtained using capillary zone electrophoresis (CZE)–MS–MS to elucidate the composition of both N- and O-linked glycopeptide oligosaccharides. Collisional activation in the orifice/skimmer region is used to generate first-generation fragment ions which undergo subsequent dissociation in the r.f.-only collision cell of the triple quadrupole mass spectrometer. These experiments provided informative peptide backbone fragment ions usually not available from fragment ion spectra of multiply protonated glycopeptide ions. These methods were applied to the characterization of α-amylase inhibitor 1, a lectin from Lotus tetragonolobus, two N-linked glycoproteins, and to κ-casein, a glycoprotein comprising O-linked sialylated glycans.
Publication date
LanguageEnglish
AffiliationNational Research Council Canada; NRC Institute for Marine Biosciences; NRC Institute for Biological Sciences
Peer reviewedNo
NRC numberBATEMAN1998
NPARC number9364905
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Record identifier42d02978-7f75-457a-942f-3a7f3f4e3711
Record created2009-07-10
Record modified2016-05-09
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