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JXB Advance Access published online on April 25, 2005
Journal of Experimental Botany, doi:10.1093/jxb/eri170
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© The Author [2005]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. For Permissions, please e-mail: journals.permissions@oupjournals.org
Received February 1, 2005
Accepted March 22, 2005

FOCUS PAPER

Thioredoxin affinity chromatography: a useful method for further understanding the thioredoxin network

Toru Hisabori 1*, Satoshi Hara 2, Tetsufumi Fujii 2, Daisuke Yamazaki 2, Naomi Hosoya-Matsuda 2, and Ken Motohashi 1

1 Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama 226-8503, Japan; ATP System Project, Exploratory Research for Advanced Technology (ERATO), Japan Science and Technology Agency (JST), 5800-3 Nagatsuta-cho, Midori-ku, Yokohama 226-0026, Japan
2 Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Midori-ku, Yokohama 226-8503, Japan

* To whom correspondence should be addressed.
Toru Hisabori, E-mail: thisabor{at}res.titech.ac.jp


  Abstract

Thioredoxin affinity chromatography can be used to recognize the target proteins of thioredoxin or thioredoxin-related proteins in whole cells or certain cellular compartments. In the last couple of years, many potential target proteins have been identified from various organelles and organisms by this method. Based on the information on the target proteins provided by these studies, the complete thioredoxin-related redox networks can now be efficiently described.

Keywords: Disulphide bond; protein-protein interaction; redox regulation; thioredoxin; thioredoxin affinity chromatography.
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