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Proteome-wide characterization of N-glycosylation events by diagonal chromatography

Bart Ghesquière (UGent) , Jozef Van Damme (UGent) , Lennart Martens (UGent) , Joël Vandekerckhove (UGent) and Kris Gevaert (UGent)
(2006) JOURNAL OF PROTEOME RESEARCH. 5(9). p.2438-2447
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Organization
Abstract
A procedure to map N-glycosylation sites is presented here. It can be applied to purified proteins as well as to highly complex mixtures. The method exploits deglycosylation by PNGase F in a diagonal, reverse-phase chromatographic setup. When applied to 10 mu L of mouse serum, affinity-depleted for its three most abundant components, 117 known or predicted sites were mapped in addition to 10 novel sites. Several sites were detected on soluble membrane or receptor components. Our method furthermore senses the nature of glycan structures and can detect differential glycosylation on a given site. These properties-high sensitivity and dependence on glycan imprinting-can be exploited for glycan-biomarker analysis.
Keywords
glycoproteome, diagonal chromatography, COFRADIC, PNGase F, HUMAN ALPHA-1-ACID GLYCOPROTEIN, HAMSTER OVARY CELLS, AMINO-ACID-SEQUENCE, MASS-SPECTROMETRY, TRIFLUOROMETHANESULFONIC ACID, LINKED OLIGOSACCHARIDES, CONGENITAL DISORDERS, HYDRAZIDE CHEMISTRY, CONTAINING PEPTIDES, SOLUBLE FORM

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Chicago
Ghesquière, Bart, Jozef Van Damme, Lennart Martens, Joël Vandekerckhove, and Kris Gevaert. 2006. “Proteome-wide Characterization of N-glycosylation Events by Diagonal Chromatography.” Journal of Proteome Research 5 (9): 2438–2447.
APA
Ghesquière, B., Van Damme, J., Martens, L., Vandekerckhove, J., & Gevaert, K. (2006). Proteome-wide characterization of N-glycosylation events by diagonal chromatography. JOURNAL OF PROTEOME RESEARCH, 5(9), 2438–2447.
Vancouver
1.
Ghesquière B, Van Damme J, Martens L, Vandekerckhove J, Gevaert K. Proteome-wide characterization of N-glycosylation events by diagonal chromatography. JOURNAL OF PROTEOME RESEARCH. 2006;5(9):2438–47.
MLA
Ghesquière, Bart, Jozef Van Damme, Lennart Martens, et al. “Proteome-wide Characterization of N-glycosylation Events by Diagonal Chromatography.” JOURNAL OF PROTEOME RESEARCH 5.9 (2006): 2438–2447. Print.
@article{356976,
  abstract     = {A procedure to map N-glycosylation sites is presented here. It can be applied to purified proteins as well as to highly complex mixtures. The method exploits deglycosylation by PNGase F in a diagonal, reverse-phase chromatographic setup. When applied to 10 mu L of mouse serum, affinity-depleted for its three most abundant components, 117 known or predicted sites were mapped in addition to 10 novel sites. Several sites were detected on soluble membrane or receptor components. Our method furthermore senses the nature of glycan structures and can detect differential glycosylation on a given site. These properties-high sensitivity and dependence on glycan imprinting-can be exploited for glycan-biomarker analysis.},
  author       = {Ghesqui{\`e}re, Bart and Van Damme, Jozef and Martens, Lennart and Vandekerckhove, Jo{\"e}l and Gevaert, Kris},
  issn         = {1535-3893},
  journal      = {JOURNAL OF PROTEOME RESEARCH},
  keyword      = {glycoproteome,diagonal chromatography,COFRADIC,PNGase F,HUMAN ALPHA-1-ACID GLYCOPROTEIN,HAMSTER OVARY CELLS,AMINO-ACID-SEQUENCE,MASS-SPECTROMETRY,TRIFLUOROMETHANESULFONIC ACID,LINKED OLIGOSACCHARIDES,CONGENITAL DISORDERS,HYDRAZIDE CHEMISTRY,CONTAINING PEPTIDES,SOLUBLE FORM},
  language     = {eng},
  number       = {9},
  pages        = {2438--2447},
  title        = {Proteome-wide characterization of N-glycosylation events by diagonal chromatography},
  url          = {http://dx.doi.org/10.1021/pr060186m},
  volume       = {5},
  year         = {2006},
}

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