Targeted quantitation of acetylated lysine peptides by selected reaction monitoring mass spectrometry

Matthew J. Rardin, Jason M. Held, Bradford W. Gibson

Research output: Chapter in Book/Report/Conference proceedingChapter

10 Scopus citations

Abstract

Mass spectrometry (MS) allows for the large-scale identification of multiple peptide analytes in complex mixtures. However, the low abundance of acetylated peptides in the overall mixture requires an enrichment step. After enrichment, the resulting acetylated peptides of interest can be quantitated using selected reaction monitoring (SRM)-MS with stable isotope dilution. Here, we describe the enrichment of lysine acetylated peptides from typsin digested mouse liver mitochondria, and the targeted quantitation of a known lysine acetylation site in succinate dehydrogenase A using SRM-MS on a triple quadrupole instrument.

Original languageEnglish
Title of host publicationSirtuins
Subtitle of host publicationMethods and Protocols
EditorsMatthew Hirschey
Pages121-131
Number of pages11
DOIs
StatePublished - Sep 20 2013
Externally publishedYes

Publication series

NameMethods in Molecular Biology
Volume1077
ISSN (Print)1064-3745

Keywords

  • Acetylation
  • Peptide immunoprecipitation
  • Selected reaction monitoring
  • Sirtuin
  • Targeted quantitation

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    Rardin, M. J., Held, J. M., & Gibson, B. W. (2013). Targeted quantitation of acetylated lysine peptides by selected reaction monitoring mass spectrometry. In M. Hirschey (Ed.), Sirtuins: Methods and Protocols (pp. 121-131). (Methods in Molecular Biology; Vol. 1077). https://doi.org/10.1007/978-1-62703-637-5_8