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. 2017 Jan 31;8:118. doi: 10.3389/fpls.2017.00118

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Copyright © 2017 Calderón, Lázaro-Payo, Iglesias-Baena, Camejo, Lázaro, Sevilla and Jiménez.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Glutathionylation of recombinant 2-Cys Prx and Prx IIF by different concentrations of GSH/GSSG. DTT-reduced Prx proteins were incubated with the different concentrations for 5 min at 37°C and the excess of glutathionylating agents was removed. A DTT-treated sample was used as negative control. Samples (15 μg protein) were immediately analyzed by western-blot using a specific monoclonal glutathione antibody, and a representative example is shown. Numbers show the mean of the densitometric analysis of at least 4 independent experiments, relative to the first band in each of the forms of the proteins. Pounceau S stained membranes were used as loading controls. Dec: decameric and Dim: dimeric forms of the proteins.