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• W2056545703 startingPage "3066" @default.
• W2056545703 abstract "Lysine-containing peptides comprising glycosylation sites derived from recombinant human erythropoietin (rHuEPO) by trypsin or Lys-C and PNGase F dual digestion were derivatized with 2-methoxy-4,5-dihydro-1H-imidazole and its deuterated analogues. In the same reaction, under reducing conditions (beta-mercaptoethanol), cysteines were converted into methyl-cysteines and lysines into Lys-4,5-dihydro-1H-imidazole. Both modifications on cysteines and lysines simplified the CID-MS/MS spectra, while preserving the structural information by yielding y-series ions and improved the mass spectral signal intensity up to 25 times. Moreover, by this approach, the N-glycan occupation sites were unambiguously determined. O-Glycosylation sites as well as O-glycan structures were determined by a LC-MS/MS experiment carried out on dually digested rHuEPO. N-Glycan mixture purified on a graphitized carbon column using a newly developed method that extracted only sialylated carbohydrates was analyzed first using MALDI-TOF in negative linear ion mode with low mass accuracy but without interferences and metastabile ions and then a reflectron with high mass accuracy. After defining the precursor ions, we performed the nanoESI QTOF MS/MS analysis on N-glycans, mainly targeting the distinction between carbohydrates with sialylated antennae and those lacking sialic acid moieties." @default.
• W2056545703 created "2016-06-24" @default.
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• W2056545703 date "2006-09-23" @default.
• W2056545703 modified "2023-10-17" @default.
• W2056545703 title "Mass Spectrometry-Based Glycoproteomic Approach Involving Lysine Derivatization for Structural Characterization of Recombinant Human Erythropoietin" @default.
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• W2056545703 doi "https://doi.org/10.1021/pr060177d" @default.
• W2056545703 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17081058" @default.
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