Proteolytic 18O labeling for comparative proteomics: model studies with two serotypes of adenovirus.

By Xudong Yao, Amy Freas, J. Ramirez, P. Demirev, C. Fenselau. Analytical Chemistry, 2001

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Mass spectrometry–based proteomics turns quantitative (2005, background): “The stable isotopes necessary for quantification can also be introduced into the peptides by the protease degrading the protein to a peptide mixtur”
Proteomics: the first decade and beyond (2003, methodology): “; 16 O or 18 O has been incorporated from H 2 16 O or H 2 18 O, respectively, at the carboxy terminus of peptides during proteolytic cleavage by trypsi”
Mapping protein post-translational modifications with mass spectrometry (2007, methodology): “Another strategy uses immobilized trypsin to catalyze O-exchange from H 2 18 O versus H 2 16 O onto C-terminal carboxylate”
Target identification with quantitative activity based protein profiling (ABPP) (2017, background): “These tags would result in mass differences that can be detected via MS, and enable quantitation and comparison across multiple samples [47–49].”
Absolute Quantification of Proteins by LCMSE (2006, methodology): “have been performed using stable isotope labeling strategies such as ICAT (3), iTRAQ (4), SILAC (stable isotope labeling by amino acids in cell culture) (5), and (18)O labeling (6, 7).”