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. 2019 Sep 16;9:13329. doi: 10.1038/s41598-019-49750-5

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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(A) Profile of a P. dicentrarchi lysate eluted through an anion exchange column (HiTrap Q) in ÄKTAprime plus (GE Healthcare) equipment. After chromatography, the fractions corresponding to the three major peaks obtained after separation of the sample (1–3) were subjected to native polyacrylamide gel electrophoresis (PAGE) staining to analyse the enzymatic activity. The enzymatic activity SOD (arrows) was located mostly in a peak (P2). (B) SOD activity observed in 12.5% native polyacrylamide gel electrophoresis (PAGE) visualized by the nitroblue tetrazolium reduction assay. In the assay, purified protein fractions, obtained by ion exchange chromatography (P2), were incubated with sodium cyanide (NaCN), hydrogen peroxide (H₂O₂), sodium azide (NaN₃) and resveratrol (RESV), or without inhibitors (control). The arrows indicate the bands of SOD activity. Mw (molecular weight).