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. 2016 Nov 10;7:1669. doi: 10.3389/fpls.2016.01669

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Copyright © 2016 Kovacs, Holzmeister, Wirtz, Geerlof, Fröhlich, Römling, Kuruthukulangarakoola, Linster, Hell, Arnold, Durner and Lindermayr.

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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Structural analysis of H₂O₂-treated GSNOR. Determination of the molecular weight of reduced (green) and oxidized (red) GSNOR using size exclusion chromatography in combination with static light scattering. The refractive index and right angle light scattering signals were monitored and used to determine the molecular weight of the reduced (black) and oxidized (gray) protein. 100 μl of the protein samples were applied to a Superdex 200 10/300 GL column. Reduced (10 mM DTT) and oxidized (1 mM H₂O₂) GSNOR were analyzed at approximately 1.5 mg/ml and both eluted as a homodimer of 90.1 and 88.4 kDa, respectively (calculated Mr is 86 kDa).