4.5 Article

Mapping O-glycosylation of apolipoprotein C-III in MALDI-FT-ICR protein profiles

Journal

PROTEOMICS
Volume 13, Issue 6, Pages 992-1001

Publisher

WILEY
DOI: 10.1002/pmic.201200293

Keywords

FT-ICR-MS; Glycomics; Glycoproteomics; High resolution proteomics; High mass accuracy; Protein profile

Funding

  1. Decrease Colorectal Cancer Death
  2. Center for Translational Molecular Medicine (CTMM)

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Ultrahigh resolution MALDI-FT-ICR profiles were obtained from human serum samples that were processed using a fully automated RPC18-based magnetic bead method. Proteins were profiled from m/z value 6630 with a resolving power of 73000 up to m/z value 12600 with a resolving power of 37000. In this study, a detailed evaluation was performed of the isoforms of apolipoprotein C-III, i.e. the different mucin-type core 1 O-glycans with the addition of one or two sialic acid residues. The MALDI-FT-ICR profiles are discussed with regard to reproducibility of the signal intensities as well as the accurate mass measurements. ESI-FT-ICR-MS/MS analyses of the same serum samples were performed to confirm the identity of apolipoprotein C-III glycoforms.

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