Abstract
A stable isotope coding strategy is described for the analysis of all types of tryptic peptides, including those that are N-terminally blocked and from the C-terminus of proteins. The method exploits differential derivatization of amine and carboxyl groups generated during proteolysis as a means of coding. Carboxyl groups produced during proteolysis incorporate 18O from H2 18O. Peptides from the C-terminus of proteins were not labeled with 18O unless they contained a basic C-terminal amino acid. Primary amines form controls, and experimental samples were differentially acylated after proteolysis with either 1H3- or 2H3-N-acetoxysuccinamide. When these two types of labeling were combined, unique coding patterns were achieved for peptides arising from the C-termini and blocked N-termini of proteins.
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Regnier, F.E. (2007). An Isotope Coding Strategy for Proteomics Involving Both Amine and Carboxyl Group Labeling. In: Sechi, S. (eds) Quantitative Proteomics by Mass Spectrometry. Methods in Molecular Biology, vol 359. Humana Press. https://doi.org/10.1007/978-1-59745-255-7_8
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DOI: https://doi.org/10.1007/978-1-59745-255-7_8
Publisher Name: Humana Press
Print ISBN: 978-1-58829-571-2
Online ISBN: 978-1-59745-255-7
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