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.
© 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Apolipoprotein C-III / blood
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Apolipoprotein C-III / chemistry*
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Apolipoprotein C-III / isolation & purification
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Carbohydrate Conformation
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Chromatography, Reverse-Phase
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Fourier Analysis
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Glycopeptides / chemistry
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Glycopeptides / isolation & purification
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Glycosylation
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Humans
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Molecular Sequence Data
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Molecular Weight
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Peptide Fragments / chemistry
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Peptide Fragments / isolation & purification
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Peptide Mapping / methods*
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Protein Isoforms / blood
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Protein Isoforms / chemistry
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Protein Isoforms / isolation & purification
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Protein Processing, Post-Translational*
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Solid Phase Extraction
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Spectrometry, Mass, Electrospray Ionization / methods
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Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / methods
Substances
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Apolipoprotein C-III
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Glycopeptides
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Peptide Fragments
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Protein Isoforms