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. 2016 Jan 4;13:1. doi: 10.1186/s12985-015-0456-4

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© León-Juárez et al. 2016

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. 6 — Analysis of NS2B protein to perform oligomerization. a The NS2B protein was incubated with different glutaraldehyde concentrations. The samples were resolved by SDS-PAGE under reducing conditions, and protein expression was analyzed by western blotting. Then, the oligomeric structures (dimers and trimers) were detected using a polyclonal antibody against the NS2B protein at a 1:3000 dilution. b Hemolysis assay results using human erythrocytes incubated with different concentrations of the NS2B or PTB proteins (5, 20, or 100 μg). The amount of hemoglobin released was analyzed by spectrophotometry. The percentage of lysis was calculated as indicated in the Materials and Methods section