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. 2018 Mar 13;8:4407. doi: 10.1038/s41598-018-22729-4

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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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Purification of the dimer mGlu₅ -∆856 produced in SF9 cells. (A) Cartoon representation of the dimer human mGlu₅ receptor (light blue) with the fusion protein eGFP (green) replacing the c-terminal domain at position 856. (B) Quantification of unpurified mGlu₅ receptor using [³H]-MPEP binding assay, measured for mGlu₅-Δ856, mGlu₅-Δ856-eGFP and mGlu₅-Δ856-eGFP (N1-N5). Dunnett’s test as part of one-way ANOVA was used for comparison with mGlu₅-Δ856 set as reference level. (C) Size exclusion chromatography profile for both constructs, mGlu₅-Δ856 (Ve = 14.5 mL) and mGlu₅-Δ856-eGFP (Ve = 14.2 mL) using superpose 6 increase. (D) Coomassie-blue stained SDS-PAGE gel of mGlu₅-Δ856 and mGlu₅-Δ856-eGFP. The gel shown is representative of three independent experiments.