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. Author manuscript; available in PMC: 2010 Aug 15.
Published in final edited form as: J Immunol Methods. 2009 Jun 16;347(1-2):3–11. doi: 10.1016/j.jim.2009.06.003

Figure 3. Immunoaffinity peptide enrichment and isotope dilution tandem mass spectrometry.

Figure 3

All proteins in the sample are digested to peptides with trypsin, which digests analyte (gray globule) and any interfering endogenous immunoglobulins (black). Stable isotope labeled peptide is added after digestion and the peptides are incubated with beads coated in polyclonal anti-peptide antibody. Unbound peptides are washed away and bound peptides are eluted and then analyzed using HPLC-tandem mass spectrometry.