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 |
|---|---|
| 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
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Ota, K., Kito, K., Iemura, S. I., Natsume, T., & Ito, T. (2008). A parallel affinity purification method for selective isolation of polyubiquitinated proteins. Proteomics, 8(15), 3004-3007. https://doi.org/10.1002/pmic.200800271