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. 2018 Jan 17;8:932. doi: 10.1038/s41598-018-19610-9

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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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S-Thiolation of rHSA by the treatment of cystine and homocystine. rHSA (150 μM) and cystine or homocystine (300 μM) were incubated at 37 °C for 24 h in 0.1 M phosphate buffer (pH 6.7) containing 0.3 M NaCl for S-thiolation of HSA. (A) HPLC chromatograph of rHSAs. rHSA (upper) and cystine (middle) or homocystine (lower) treated rHSA was analyzed by anion-exchange chromatography by monitoring the excitation at 280 nm and emission at 340 nm. (B) and (C) Detection of free cysteine residue. rHSA and cystine (B) or homocystine (C) treated rHSA were labeled with biotin-maleimide and subjected to non-reducing SDS-PAGE followed by immunoblot analysis. (D) Identification of S-thiolated cysteine residue of cystine or homocystine treated rHSA.