Structural analysis of 2D-gel-separated glycoproteins from human cerebrospinal fluid by tandem high-resolution mass spectrometry
(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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https://lup.lub.lu.se/record/4bf893b7-614c-4304-ae07-10d1532c9337
- author
- Håkansson, Kristina ; Emmett, Mark R ; Marshall, Alan G ; Davidsson, Pia and Nilsson, Carol L LU
- publishing date
- 2003-12-25
- 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 (ACS)
- external identifiers
-
- scopus:0348142992
- pmid:14692451
- 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
- 2024-01-28 18:25:32
@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 (<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}}, 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.}}, language = {{eng}}, month = {{12}}, number = {{6}}, pages = {{8--581}}, publisher = {{The American Chemical Society (ACS)}}, 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}}, doi = {{10.1021/pr034030n}}, volume = {{2}}, year = {{2003}}, }