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. 2019 Mar 11;18:47. doi: 10.1186/s12934-019-1094-0

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© The Author(s) 2019

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. 5 — Disulphide bond formation in Nb-HlyA fusions. Thiol alkylation assay to determine the oxidation state of Cysteines (Cys) in secreted and cytoplasmic Nb-HlyA fusions from TD4 and TF1 clones, containing 2 and 4 Cys residues, respectively. Secreted proteins in culture supernatants and bacterial samples are treated (+) or not (−) with AMS (alkylating agent) and DTT (reducing agent), as indicated. Retarded mobility of alkylated polypeptides is indicative of reduced thiol groups. Protein bands of Nb-HlyA fusions developed after non-reducing SDS-PAGE and Western blot with anti-E-tag mAb