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Characterisation of tyrosine phosphorylations induced in immune cells in response to inflammatory stimuli may help elucidate the molecular bases of the diversity of immune responses. We have used anti-phosphotyrosine antibodies in combination with cell surface biotinylation in a two-step affinity purification procedure to recover pervanadate-induced tyrosine phosphorylated proteins from sub-cellular compartments, including the cell surface, of murine T cells and macrophages prior to separation by solution-phase isoelectric focussing and one-dimensional gel electrophoresis and identification by tandem mass spectrometry.

Original publication




Journal article



Publication Date





2417 - 2421


Animals, Antibodies, Biotinylation, Cell Compartmentation, Cell Line, Electrophoresis, Polyacrylamide Gel, Hybridomas, Immunoprecipitation, Isoelectric Focusing, Macrophages, Mass Spectrometry, Membrane Proteins, Mice, Phosphoproteins, Phosphorylation, Phosphotyrosine, Protein Tyrosine Phosphatases, Proteome, T-Lymphocytes, Vanadates