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. 2016 Dec 6;7:1817. doi: 10.3389/fpls.2016.01817

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Copyright © 2016 López-Castillo, Jiménez-Sandoval, Baruch-Torres, Trasviña-Arenas, Díaz-Quezada, Lara-González, Winkler and Brieba.

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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Differential effect of GSSG on the enzymatic activity of AtTPIs and dimer stability. (A) Effect of GSSG on the enzymatic activity of cTPI (red) and pdTPI (green) after 3 h of incubation at 25°C with increasing concentrations of oxidized glutathione (0–25 mM). The results are expressed as a percentage of the activity with respect to the untreated protein sample. (B,C) Effect of addition of GSSG on the oligomerization of AtTPIs. (B) Size-exclusion profile showing the effect of the addition of GSSG on cTPI dimer stability. The non-derivatized enzyme is shown in red, whereas the GSSG incubated enzyme is shown in black. The SDS-PAGE shows the molecular weight of collected fractions of the cTPI-GSSG peak. (C) Size-exclusion profile showing the effect of the addition of GSSG on the pdTPI oligomeric profile. The non-derivatized enzyme is shown in green and the GSSG treated enzyme is shown in black. The SDS-PAGE shows the molecular weight of collected fractions of the pdTPI-GSSG peak. The elution profiles for MW standards; thyroglobulin (670 kDa), γ-globulin (158 kDa), ovalbumin (44 kDa), myoglobin (17 kDa), and vitamin B12 (1.35 kDa) are represented as dots.