Exploring the binding profiles of ConA, boronic acid and WGA by MALDI-TOF/TOF MS and magnetic particles.
Concanavalin A, boronic acid and Wheat germ agglutinin functionalized magnetic micro-particles were developed to enrich glycosylated peptides and proteins. The bead functionalities were validated according to their specificity by analyses of model proteins. Validated beads were employed for the enrichment of glycosylated human serum proteins. Eluted glycoproteins were digested by trypsin and the resulting peptides were purified by magnetic MB-HIC C8 beads. Each fraction was analyzed by MALDI-TOF MS and single peaks were subjected to MALDI-TOF/TOF MS with the objective to identify the respective proteins by database search. Search results revealed overlapping profiles of known serum glycoproteins.
Sparbier
Katrin
K
Bruker Daltonik GmbH, Permoserstrasse 15, 04318 Leipzig, Germany. KSP@BDAL.de
Wenzel
Thomas
T
Kostrzewa
Markus
M
D001798:Blood Proteins / Q000378:metabolism; D001897:Boronic Acids / Q000378:metabolism*; D003208:Concanavalin A / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D006031:Glycosylation; D008280:Magnetics; D010449:Peptide Mapping; D011485:Protein Binding; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods*; D014909:Wheat Germ Agglutinins / Q000378:metabolism*
D001798:Blood Proteins; D001897:Boronic Acids; D006023:Glycoproteins; D014909:Wheat Germ Agglutinins; D003208:Concanavalin A