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. 2019 Jun 14;9:8631. doi: 10.1038/s41598-019-45003-7

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© The Author(s) 2019

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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Identification of Steroleosin B as a sesamin-binding protein and purification of recombinant GST-fused Steroleosin B. (a) Reaction conditions for the synthesis of sesamin probe 4; (i) DIBAL, toluene, reflux, 1 h; (ii) BrCH₂CO₂Me, K₂CO₃, DMF, rt, 1 h; (iii) 1 N NaOH aq., THF, rt, 1 h. (b) Structure of LD- or HD-SIB and AIB. (c) Lysates from sesame seedlings in the absence (lanes 1 and 3) or presence (lanes 2 and 4) of sesamin were incubated with LD-SIB (lanes 1 and 2) or HD-SIB (lanes 3 and 4). The proteins eluted from SIB were resolved using sodium dodecyl sulfate-poly acrylamide gel electrophoresis (SDS-PAGE) and were then subjected to silver staining. The band marked by the arrow (lane 3 in magnified image) was diminished in the presence of sesamin as a competitor (lane 4). (d) Whole cell extracts of E. coli producing recombinant GST-fused Steroleosin B were incubated with AIB or SIB. The resulting eluents were resolved using SDS-PAGE followed by silver staining. The arrows in SDS-PAGE show the bands for GST-fused Steroleosin B.