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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) SDS-PAGE and (B) Western blot of purified prBChE protein compared to serial dilutions of PEG-rBChE protein control. (A) Coomassie stained gel: lanes 1 and 2 contain duplicate loadings of 7 μg of prBChE protein. Lanes 3 to 6 contain serial dilutions of PEG-rBChE control (lane 3: 1, lane 4: 3, lane 5: 7, and lane 6: 10 μg), all loaded under reduced conditions. Lane M shows the pre-stained protein molecular weight standards along with the molecular weight in kDa. Because the goat recombinant BChE is PEGylated, its monomeric mobility on SDS-PAGE is approximately 200 kDa. However, the unPEGylated goat BChE co-migrates with prBChE as revealed by SDS-PAGE. (B) Western blot analysis using 1:200 mouse anti-BChE antibody and 1:2,000 goat anti-mouse HRP conjugated antibody.