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. 2016 Jun 16;7:743. doi: 10.3389/fpls.2016.00743

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Copyright © 2016 Alkanaimsh, Karuppanan, Guerrero, Tu, Hashimoto, Hwang, Phu, Arzola, Lebrilla, Dandekar, Falk, Nandi, Rodriguez and McDonald.

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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(A) Western blot analysis of a native gel of crude preparation of prBChE. Western blot analysis was performed using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody of crude extract preparation of 0.25 μg prBChE (lane 3) compared to 0.25 μg of equine control (lane 1) and 0.25 μg pure prBChE protein (lane2). (B) Native gel analysis of different prBChE variants. 45 mU of prBChE-ER (lane 1), prBChE (lane 2), prBChE-AWF (lane 3) and equine control (lane 4) were loaded to a 7.5% gel and stained for BChE activity according to the method of Karnovsky and Roots (1964).