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. 2020 Apr 27;14(4):e0008269. doi: 10.1371/journal.pntd.0008269

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© 2020 Xu et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 4 — A-B Hydrolysis of Hb by rTsASP2 at different pH values. A: human Hb; B: mouse Hb; M: protein marker; lanes 1, 3, 5 and 7: Hb alone; lanes 2, 4, 6 and 8: Hb+ rTsASP2; lanes 1 and 2: pH 2.5; lanes 3 and 4: pH 3.5; lanes 5 and 6: pH 4.5; lanes 7 and 8: pH 5.5. C: Hydrolysis efficiency effect of rTsASP2 on mouse Hb (pH 2.5). M: protein marker; lanes 1, 3, 5 and 7: Hb alone; lanes 2, 4, 6 and 8: Hb+ rTsASP2; lanes 1 and 2: 5 min; lanes 3 and 4: 30 min; lanes 5 and 6: 90 min; lanes 7 and 8: 4 h. D: Inhibition effect of anti-rTsASP2 serum and pepstatin A on rTsASP2 hydrolysis of mouse Hb (pH 2.5). M: protein marker; lane 1: rTsASP2; lane 2: anti-rTsASP2 serum; lane 3: heated anti-rTsASP2 serum; lane 4: Hb; lane 5: Hb +rTsASP2; lane 6: anti-rTsASP2 serum pre-incubated with rTsASP2 +Hb; lane 7: heated anti-rTsASP2 serum pre-incubated with rTsASP2+ Hb; lane 8: pepstatin A pre-incubated with rTsASP2 + Hb. The arrow represents the band of rTsASP2 (86.4 kDa).