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A Parallel Affinity Purification Method for Selective Isolation of Polyubiquitinated Proteins by Kazuhisa Ota; Keiji Kito; Shun‐ichiro Iemura; Tohru Natsume; Takashi Ito is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## 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.

Who reads A Parallel Affinity Purification Method for Selective Isolation of Polyubiquitinated Proteins?

Author

Kazuhisa Ota; Keiji Kito; Shun‐ichiro Iemura; Tohru Natsume; Takashi Ito

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Ltd.; Wiley; Research Square (ISSN 1615-9853)

Published

2008

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)