Separation and Purification of multiply acetylated proteins using cation-exchange chromatography

Romeo Papazyan, Sean D. Taverna

Research output: Chapter in Book/Report/Conference proceedingChapter

4 Scopus citations


High-performance liquid chromatography (HPLC) is extremely useful for the study of proteins and the characterization of their posttranslational modifications. Here we describe a method that utilizes cationexchange HPLC to separate multiply acetylated histone H3 species on the basis of their charge and hydrophilicity. This high-resolution method allows for the separation of histone H3 species that differ by as few as one acetyl group, and is compatible with subsequent analysis by a variety of techniques, including mass spectrometry and western blotting.

Original languageEnglish (US)
Title of host publicationProtein Acetylation
Subtitle of host publicationMethods and Protocols
PublisherHumana Press Inc.
Number of pages11
ISBN (Print)9781627033046
StatePublished - 2013

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Acetic anhydride
  • Acetylation
  • Cation-exchange chromatography
  • HPLC
  • Histone H3
  • PolyCAT A

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics


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