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• W2312692361 endingPage "3483" @default.
• W2312692361 startingPage "3474" @default.
• W2312692361 abstract "Reversible phosphorylations play a critical role in most biological pathways. Hence, in signaling studies great effort has been put into identification of a maximum number of phosphosites per experiment. Mass spectrometry (MS)-based phosphoproteomics approaches have been proven to be an ideal analytical method for mapping of phosphosites. However, because of sample complexity, fractionation of phosphopeptides prior to MS analysis is a crucial step. In the current study, we compare the chromatographic strategies electrostatic repulsion-hydrophilic interaction chromatography (ERLIC), hydrophilic interaction liquid chromatography (HILIC), and strong cation exchange chromatography (SCX) for their fractionation behavior of phosphopeptides. In addition, we investigate the use of repetitive TiO(2)-based enrichment steps for a maximum identification of phosphopeptides. On the basis of our results, SCX yields the highest number of identified phosphopeptides, whereas ERLIC is optimal for the identification of multiphosphorylated peptides. Consecutive incubations of fractions and flow-through by TiO(2) beads enrich qualitatively different sets of phosphopeptides, increasing the number of identified phosphopeptides per analysis." @default.
• W2312692361 created "2016-06-24" @default.
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• W2312692361 date "2011-07-08" @default.
• W2312692361 modified "2023-10-10" @default.
• W2312692361 title "Comparison of ERLIC–TiO₂, HILIC–TiO₂, and SCX–TiO₂ for Global Phosphoproteomics Approaches" @default.
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• W2312692361 doi "https://doi.org/10.1021/pr200092z" @default.
• W2312692361 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21682340" @default.
• W2312692361 hasPublicationYear "2011" @default.
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