Journal article
A parallel affinity purification method for selective isolation of polyubiquitinated proteins
Department of Computational Biology, Graduate School of Frontier Sciences, University of Tokyo, Kashiwa, Japan.1
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.
Language: | English |
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Publisher: | WILEY-VCH Verlag |
Year: | 2008 |
Pages: | 3004-3007 |
ISSN: | 16159861 and 16159853 |
Types: | Journal article |
DOI: | 10.1002/pmic.200800271 |