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. 2011 Sep 23;63(1):365–379. doi: 10.1093/jxb/err282

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© 2011 The Author(s).

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

This paper is available online free of all access charges (see http://jxb.oxfordjournals.org/open_access.html for further details)

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Fig. 4. — Chaperone foldase activity of chloroplastic tobacco Trx f and Trx m. The Cys-free form of G6PDH (20 μM) was denatured in guanidine-HCl and subsequently refolded in a renaturation buffer in the presence of increasing concentrations of Trx f (closed circles) or Trx m (closed squares) as indicated. The refolding yield of G6PDH was determined by measuring G6PDH activity and expressed as a percentage of native G6PDH activity set to 100%. Reactions using analogous concentrations of BSA (crosses) instead of Trx were used as controls. Each value is the mean ±SE (bars) of three independent determinations.