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Structural analysis of 2D-gel-separated glycoproteins from human cerebrospinal fluid by tandem high-resolution mass spectrometry

Håkansson, Kristina; Emmett, Mark R; Marshall, Alan G; Davidsson, Pia and Nilsson, Carol L LU (2003) In Journal of Proteome Research 2(6). p.8-581
Abstract

The feasibility of global glycoprotein analysis by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry and infrared multiphoton dissociation (IRMPD) tandem mass spectrometry is demonstrated. Combined 2D gel glycoprotein separation and visualization, in-gel digestion, and accurate (<10 ppm) mass measurement allowed identification of human glycoproteins and revealed differences in glycosylation. IRMPD obviates the need for glycan release, which prevents sample dispersal, and allows the assignment of glycan structures to specific sites of N-glycosylation.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Carbohydrate Conformation, Carbohydrate Sequence, Electrophoresis, Gel, Two-Dimensional, Glycoproteins, Humans, Mass Spectrometry, Molecular Sequence Data, Peptides, Protein Conformation, Protein Isoforms, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, Non-P.H.S.
in
Journal of Proteome Research
volume
2
issue
6
pages
8 pages
publisher
The American Chemical Society
external identifiers
  • scopus:0348142992
ISSN
1535-3893
DOI
10.1021/pr034030n
language
English
LU publication?
no
id
4bf893b7-614c-4304-ae07-10d1532c9337
date added to LUP
2017-05-16 10:37:22
date last changed
2018-10-03 10:11:15
@article{4bf893b7-614c-4304-ae07-10d1532c9337,
  abstract     = {<p>The feasibility of global glycoprotein analysis by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry and infrared multiphoton dissociation (IRMPD) tandem mass spectrometry is demonstrated. Combined 2D gel glycoprotein separation and visualization, in-gel digestion, and accurate (&lt;10 ppm) mass measurement allowed identification of human glycoproteins and revealed differences in glycosylation. IRMPD obviates the need for glycan release, which prevents sample dispersal, and allows the assignment of glycan structures to specific sites of N-glycosylation.</p>},
  author       = {Håkansson, Kristina and Emmett, Mark R and Marshall, Alan G and Davidsson, Pia and Nilsson, Carol L},
  issn         = {1535-3893},
  keyword      = {Carbohydrate Conformation,Carbohydrate Sequence,Electrophoresis, Gel, Two-Dimensional,Glycoproteins,Humans,Mass Spectrometry,Molecular Sequence Data,Peptides,Protein Conformation,Protein Isoforms,Journal Article,Research Support, Non-U.S. Gov't,Research Support, U.S. Gov't, Non-P.H.S.},
  language     = {eng},
  month        = {12},
  number       = {6},
  pages        = {8--581},
  publisher    = {The American Chemical Society},
  series       = {Journal of Proteome Research},
  title        = {Structural analysis of 2D-gel-separated glycoproteins from human cerebrospinal fluid by tandem high-resolution mass spectrometry},
  url          = {http://dx.doi.org/10.1021/pr034030n},
  volume       = {2},
  year         = {2003},
}