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. 2019 May 8;10:583. doi: 10.3389/fpls.2019.00583

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Copyright © 2019 Pei, Li, Zhu, Ge, Sun, Liu, Jia, Li and Hou.

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) and the copyright owner(s) 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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Structure predictions of GhABP19 and its SOD activity. (A,B) Modelings of Hordeum vulgare germin protein (A) and GhABP19 protein (B). The H. vulgare germin amino acids–His88, His90, His137, and Glu97 and GhABP19 amino acids–His137, His139, His183, and Glu144 responsible for SOD domain are highlighted. (C) SOD activity of purified GhABP19 protein. 4.4, 8.1, 12.4, and 16.0 μg of purified GhABP19 protein was used in this assay. Commercial bovine erythrocyte Cu/Zn-SOD was used as positive control. Error bars represent standard error and shown for three replicates.