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. 2014 Apr 3;9(4):e92411. doi: 10.1371/journal.pone.0092411

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© 2014 Brizuela 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 properly credited.

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(A) Immunoblot analysis of saponin-purified P. falciparum parasites (strain 3D7) and uninfected erythrocytes (separated under reducing conditions) for Prx2, hyperoxidized Prx (Prx-SO2/3) and hexokinase. Equal numbers of cells were loaded in each lane. The presence of human hexokinase indicates the relative level of contaminating red cell proteins in the purified parasite fraction. (B and C) Immunoblot analysis of the effect of BBMQ treatment of human erythrocytes on Prx2 multimer formation using anti-Prx2 antibody (B), and on total and hyperoxidized amounts of Prx2 (C), using the respective antibodies. In (B) proteins were extracted in the presence of N-ethylmaleimide and separated under non-reducing conditions. In (C) proteins were separated under reducing conditions.