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 language | English |
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Pages (from-to) | 3004-3007 |
Number of pages | 4 |
Journal | Proteomics |
Volume | 8 |
Issue number | 15 |
DOIs | |
Publication status | Published - Aug 1 2008 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology