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. 2020 Feb 3;10:1659. doi: 10.1038/s41598-020-57671-x

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© The Author(s) 2020

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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SDS-PAGE gels of pro-jrPPO1-wt after digestion with A) trypsin, B) nagarse and C) proteinase K under reducing conditions. Lane M = marker, lane 1 = jrPPO1-wt without protease, lanes 2–5 = wild-type with protease (1% w/w) after 1, 2, 3 and 5 minutes. The red box highlights the still intact C-terminal domain and the black box highlights the band representing the active enzyme. Trypsin digestion (A) resulted in one sharp band for the active enzyme, thus indicating specific cleavage, whereas nagarse (B) and proteinase K (C) led to a more diffuse band pattern, indicating cutting at several positions. The gels were cropped to display the lanes of interest. (full-length gels: Fig. S24).