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. 2018 Dec 12;11:629. doi: 10.1186/s13071-018-3251-4

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© The Author(s). 2018

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. 5 — Ion-dependent DNase activity of PkTatD. a PkTatD-GST recombinant protein at concentrations from 0 to 5 μM was incubated with 200 ng of DNA in PBS (pH 7.4) at 37 °C for 1 h. DNA was completely hydrolyzed at a concentration of 3 μM. GST protein was used as a negative control. b DNA was completely hydrolyzed at 35 °C and the enzyme remained active at 41 °C. c PkTatD-GST recombinant protein and DNA were incubated with divalent metal ions at concentrations from 0 to 10 mM. The enzyme activity was enhanced by Mg²⁺ but inhibited by Cu²⁺. d Mg²⁺ (10 mM) and DNA were incubated with recombinant PkTatD-GST protein at concentrations from 0 to 5 μM