Structural analysis of 2D-gel-separated glycoproteins from human cerebrospinal fluid by tandem high-resolution mass spectrometry.
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.
Håkansson
Kristina
K
Ion Cyclotron Resonance Program, National High Magnetic Field Laboratory, Florida State University, 1800 East Paul Dirac Drive, Tallahassee, Florida 32310-3706, USA.
Emmett
Mark R
MR
Marshall
Alan G
AG
Davidsson
Pia
P
Nilsson
Carol L
CL
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D015180:Electrophoresis, Gel, Two-Dimensional; D006023:Glycoproteins / Q000134:cerebrospinal fluid* / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D008969:Molecular Sequence Data; D010455:Peptides / Q000134:cerebrospinal fluid / Q000737:chemistry / Q000378:metabolism; D011487:Protein Conformation; D020033:Protein Isoforms / Q000134:cerebrospinal fluid / Q000737:chemistry / Q000378:metabolism
D006023:Glycoproteins; D010455:Peptides; D020033:Protein Isoforms