Abstract
This chapter discusses the use of mass spectrometry (MS) for the detection and characterization of posttranslational modifications. Protein isolation procedures may induce the deamidation of asparagine or glutamine residues and the oxidation of methionine residues, or the inadvertent cleavage of the peptide sequence by contaminating proteins. The use of electrospray ionization (ESI) can characterize intact proteins whereas HPLC-ESI-MS can characterize peptides produced by trypsin digestion of proteins. Phosphorylated peptides are characterized after chromatography on metal ion chelating columns. Proteins are desalted by reverse-phase HPLC in aqueous acetonitrile or methanol solutions. These solvents can be infused directly into the mass spectrometer. Alternatively, proteins can be lyophilized from ammonium bicarbonate, ammonium acetate, or N-ethyl morpholine solutions.
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