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. 2017 Oct 25;7:14053. doi: 10.1038/s41598-017-13784-4

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© The Author(s) 2017

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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Binding stoichiometry of NP-UAP56 complex. (a) SDS-PAGE analysis. The detail of purification scheme is described in Methods. Lane 1, molecular size marker; Lane 2, NP-His; Lane 3, UAP56. (b) Gel filtration chromatography. NP-UAP56 complex was partially purified using Sephacryl S-200 gel filtration column. Then, the purified NP-UAP56 complex (black), UAP56 (red), and NP (blue) were eluted from a Superose 6 gel filtration column. The peak positions of protein standards are marked by arrows. (c) NP (300 ng), UAP56 (300 ng), and NP-UAP56 complex (66, 200, and 600 ng) were separated on 10% SDS-PAGE and visualized by CBB staining. (d) UAP56, NP, and NP-UAP56 complex were analyzed by 6% native PAGE in 0.5 × TBE buffer and visualized by silver staining.