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Proteomics. 2013 Mar;13(6):992-1001. doi: 10.1002/pmic.201200293. Epub 2013 Feb 19.

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

Author information

1
Center for Proteomics and Metabolomics, Leiden University Medical Center (LUMC), Leiden, The Netherlands.

Abstract

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 73 000 up to m/z value 12 600 with a resolving power of 37 000. 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.

PMID:
23335445
DOI:
10.1002/pmic.201200293
[Indexed for MEDLINE]

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