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Research in-depth qualitative and quantitative profiling of tyrosine phosphorylation using a combination of phosphopeptide immunoaffinity purification and stable isotope dimethyl labeling * □s.
| Content Provider | CiteSeerX |
|---|---|
| Author | Boersema, Paul J. Foong, C. Leong Yan Ding, D. Vanessa M. Y. Lemeer, D. Simone Breukelen, Bas Van Philp, B. Robin Boekhorst, D. Jos Snel, F. Berend Hertog, Jeroen Den Choo, H. Andre B. H. Albert J. R. Heck, A. |
| Abstract | Several mass spectrometry-based assays have emerged for the quantitative profiling of cellular tyrosine phosphorylation. Ideally, these methods should reveal the exact sites of tyrosine phosphorylation, be quantitative, and not be cost-prohibitive. The latter is often an issue as typically several milligrams of (stable isotope-labeled) starting protein material are required to enable the detection of low abundance phosphotyrosine peptides. Here, we adopted and refined a peptidecentric immunoaffinity purification approach for the quantitative analysis of tyrosine phosphorylation by combining it with a cost-effective stable isotope dimethyl labeling method. We were able to identify by mass spectrometry, using just two LC-MS/MS runs, more than 1100 unique non-redundant phosphopeptides in HeLa cells from about 4 mg of starting material without |
| File Format | |
| Access Restriction | Open |
| Subject Keyword | Tyrosine Phosphorylation Quantitative Profiling Research In-depth Qualitative Stable Isotope Dimethyl Labeling Phosphopeptide Immunoaffinity Purification Protein Material Quantitative Analysis Several Milligram Cellular Tyrosine Phosphorylation Hela Cell Spectrometry-based Assay Exact Site Cost-effective Stable Isotope Dimethyl Mass Spectrometry Low Abundance Phosphotyrosine Peptide Lc-ms M Unique Non-redundant Phosphopeptides Peptidecentric Immunoaffinity Purification Approach |
| Content Type | Text |
