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. 2021 Jan 15;10:585986. doi: 10.3389/fcimb.2020.585986

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Copyright © 2021 Zhang, Li, El Moussawi, Saab, Zhang, Osta and Michel

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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Active CLIPB10_Xa is inhibited by rSRPN2. (A) SDS-PAGE and Coomassie blue staining shows the presence of a covalent complex formed by rCLIPB10_Xa and rSRPN2, indicated by asterisk. CLIPB10_Xa zymogen is indicated by a filled star, catalytic domain is indicated by an open star, factor Xa is indicated by diamond, and rSRPN2 is indicated by triangle. (B) IEARpNa was used as the substrate to measure the residual amidase activity of active CLIPB10_Xa, which was inhibited by rSRPN2 at increasing molar ratios. Data are shown as means ± S.D. (n = 3). The stoichiometry of inhibition is 1.89.