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. 2017 Jul 24;7:6312. doi: 10.1038/s41598-017-06395-6

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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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Immunoaffinity purification of the myospryn complex from cardiac muscle. (a) Proteins eluted from an anti-minispryn immunoaffinity column or protein G only column were separated by PAGE and stained with colloidal Coomassie blue dye. Bands A1-A3 that were only present in minispryn immunoaffinity eluate were excised and processed for mass spectrometry. The identity of the major protein(s) found in each band is listed. Note that in this study we focussed exclusively on proteins in bands A1, A2 and A3. Corresponding peptides for myospryn, RyR2 and minispryn are shown in Supplementary Dataset 1. (b) Robust minispryn enrichment following immunoaffinity purification was demonstrated by immunoblotting using the 819 anti-minispryn antibody. The sizes of the molecular weight markers are shown in kDa.