A parallel affinity purification method for selective isolation of polyubiquitinated proteins

Kazuhisa Ota, Keiji Kito, Shun Ichiro Iemura, Tohru Natsume, Takashi Ito

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

We developed a parallel affinity purification (PAP) procedure, in which ubiquitinated proteins are purified from the cells that coexpress two affinity-tagged ubiquitins by sequential use of affinity chromatography specific to each tag. In contrast with previous procedures using a single affinity-tagged ubiquitin, the PAP eliminates highly abundant ubiquitin monomers and monoubiquitinated proteins to selectively enrich proteins bearing both affinity-tags, or poly- and multiubiquitinated proteins. Accordingly, it would serve as a powerful method to facilitate mass-spectrometric identification of ubiquitinated proteins.

Original languageEnglish
Pages (from-to)3004-3007
Number of pages4
JournalProteomics
Volume8
Issue number15
DOIs
Publication statusPublished - Aug 1 2008
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology

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