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. 2015 Jul 16;14:104. doi: 10.1186/s12934-015-0271-z

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© Samazan et al. 2015

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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SEC-MALS analysis of purified rHtrA proteins. SEC-MALS analysis of (a) purified rHtrA₁ (40 kDa) and (b) rHtrA₂ (39 kDa), proteins is shown. rHtrA proteins at 1 mg/mL (small dash line), 2 mg/mL (large dash line) and 4 mg/mL (solid line) were loaded on a 15 mL KW-803 column (Shodex). Absorbance at 280 nm (on the left) and molar mass (on the right) are plotted as a function of the elution volume. Results obtained with rHtrA₁ were confirmed using a Superdex 200 increase 10/300 GL column (GE, data not shown). RU relative unit.