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

Romeo Papazyan, Sean D. Taverna

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

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.
Pages103-113
Number of pages11
ISBN (Print)9781627033046
DOIs
StatePublished - 2013

Publication series

NameMethods in Molecular Biology
Volume981
ISSN (Print)1064-3745

Keywords

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

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

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