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. 2018 Apr 26;8:6614. doi: 10.1038/s41598-018-24688-2

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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 images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Hemolytic activity of monomer and dimer StI W111C forms. Time course of erythrocyte lysis of homodimer (A) and monomer (B) at different concentrations by measuring the decrease in the turbidity (DO_{600 nm}) of an erythrocyte suspension. (C) dependence of the haemolytic rate respect to monomer and dimer concentrations. The kinetic parameters t_1/2 (time when the initial DO_{600 nm} value of the erythrocyte suspension is reduced to the half) was estimated from curves on panels A and B. Rate of hemolysis is expressed as the reciprocal of the half-time of hemolysis (t_1/2). (D) The percentage of hemolysis of dimer (without 2-ME) and monomer (dimer incubate with 0.1 M of 2-ME for 24 h) was determined for various doses of the toxin. The HC₅₀ (concentration where 50% of HRBC are lysed after 15 min) of dimer (solid squares) and monomer (open squares) calculated from the best sigmoidal fit (dash lines) are shown in the inserted table. In panels C and D are shown the means and standard errors from 3–5 independent experiments.