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. 2019 Jul 19;19:146. doi: 10.1186/s12862-019-1465-5

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© The Author(s). 2019

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 2 — PAGE analysis of APX activity and protein during the purification of APX activity. Peak APX fractions were separated by nondenaturing 10% PAGE. a Gel stained with Coomassie blue. b APX activity was visualized by a nitroblue tetrazolium stain. Lanes 1: Peak APX fraction from DEAE sephacel (30 μg protein). Lanes 2: Peak APX fraction from phenyl Sepharose, Lanes 3: The fraction following the APX peak activity from phenyl Sepharose. c SDS-PAGE analysis of peak APX fraction. d Sequences of tryptic peptides identified by Edman degradation from the 32 kDa band in (c)