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. 2016 Aug 11;16:183. doi: 10.1186/s12866-016-0802-8

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© The Author(s). 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 the interaction between BslA_(260–652) and laminin. a ELISA analysis of the binding of different concentrations of BslA_(260–652) to immobilized laminin. b ELISA analysis of the binding of different concentrations of laminin to immobilized BslA_(260–652) with and without the presence of an excess of BslA_(260–652) in solution. Responses at equilibrium of the ELISA curves were fit to a one-site binding (hyperbola) isotherm (GraphPad Prism 5). All values are the averages of repeat experiments performed in triplicate with the background absorption subtracted. Error bars indicate SEM