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. 2019 Jul 23;10:1707. doi: 10.3389/fimmu.2019.01707

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Copyright © 2019 Chen, Tian, Hou, Li, Tian, Yuan, Li, Elsheikha and Zhu.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Fasciola gigantica-derived rFgCatB enzymatic activity was determined by examining its ability to cleave the fluorescent synthetic substrate RR-AFC to release free AFC. The enzyme activity of rFgCatB was measured by Cathepsin B Activity Assay Kit as described in the materials and methods and the result showed a high activity of the rFgCatB (t-test, t = 72.68, P < 0.0001). Asterisks indicate statistical significance between rFgCatB sample and cathepsin B inhibitor-treated control sample (^****P < 0.0001).