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• W2045350566 abstract "We applied the improved sensitivity and soft ionization characteristics of electrospray Ionization (ESI)S/MS and matrix-assisted laser desorption/ionization(MALDI)-time of flight (TOF) mass spectrometry (MS) to analysis of the GPI-anchored C-terminal peptide derived from 5′ -nucleotidase. ESI-MS/MS analysis was applied to the core structure (MW, 2, 743). In the collision-induced dissociation (CED) spectrum, single-charged ions such as m/z 162 (glucosamine), 286 (mannose-phosphate-ethanolamine), and 447 ([mannose-phos-phate-ethanolamine] -glucosamine) were clearly detected as characteristic fragment ions of the GPI-anchored peptide. On MALDI-TOF-MS analysis, heterogeneous peaks of GPI-anchored peptides were detected as single-charged ions in the positive mode. Product ions were obtained by post-source decay (PSD) of m/z 2, 905 using curved field reflectron of TOF-MS. Most of the expected product ions derived from the GPI-anchored peptide, containing the core structure and an additional mannose side chain, were successively obtained. Thus, ESI-MS/MS and MALDI-TOF-PSD-MS proved to be effective and sensitive methods for analyzing the GPI-anchored peptide structure with less than 10 pmol of sample. These characteristic fragments or fragmentation patterns seem to be very useful for identification of GPI-anchored C-terminal peptides derived from any kind of GPI-anchored protein." @default.
• W2045350566 created "2016-06-24" @default.
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• W2045350566 date "1999-08-01" @default.
• W2045350566 modified "2023-10-17" @default.
• W2045350566 title "Application of Electrospray Ionization MS/MS and Matrix-Assisted Laser Desorption/Ionization-Time of Flight Mass Spectrometry to Structural Analysis of the Glycosyl-Phosphatidylinositol-anchored Protein" @default.
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• W2045350566 doi "https://doi.org/10.1093/oxfordjournals.jbchem.a022467" @default.
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