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. 2017 Jul 19;23:35. doi: 10.1186/s40409-017-0125-8

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© The Author(s). 2017

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. 3 — The catalytic activity of NnV on several chromogenic substrates. a NnV was preincubated with different substrates [N-Succinyl-Ala-Ala-Ala-ρNA (for elastase), Nα-Benzoyl-DL-Arg-ρNA (for trypsin), N-(p-Tosyl)-Gly-Pro-Lys-ρNA·acetate salt (for plasmin), N-Benzoyl-Phe-Val-Arg-ρNA·HCl (for thrombin), N-Succinyl-Ala-Ala-Pro-Phe-ρNA (for chymotrypsin)], 0.5 mM for 1 h. The catalytic activity of NnV was assayed at 405 nm. b NnV was preincubated with different protease inhibitors (1 mM), followed by reacting chymotrypsin substrate for 30 min. Data represent as mean ± SD from the three fields *p < 0.05 and **p < 0.01, compared to control