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. 2019 Mar 4;9:3359. doi: 10.1038/s41598-019-40044-4

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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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Affinity chromatography of biotinylated proteins using M18-L-DBD matrix. (a) Biotinylated bovine serum albumin (BSA) with 12 biotin moieties per molecule. Overloading amount of biotinylated BSA was applied. Fractions were analyzed by SDS-PAGE. Closed arrowhead, biotinylated BSA; Open arrowhead, Sephadex bound M18-L-DBD. (b) Biotinylated human fibroblast growth factor (FGF) with 4.8 biotin moieties per protein. Pure chemically biotinylated human FGF was mixed with the E. coli soluble fraction to constitute the crude sample. Fractions were analyzed by SDS-PAGE. Closed arrowhead, biotinylated FGF. M, molecular weight markers (sizes in kDa); S, loaded sample; FT, flow-through fraction; W, wash fractions; E, elution fractions; BF, bound fraction. Gel profiles shown in panels a and b are from different gels.