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. 2019 Oct 11;10:4656. doi: 10.1038/s41467-019-12672-x

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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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Fig. 3 — Online 2D-LC-MS/MS proteomics analysis of liver and kidney proteins. Biotinylated proteins from one liver and one kidney samples were enriched on streptavidin columns, trypsinized and subjected to an online 2D-LC-MS/MS workflow on a C18 column at high/low pH. Total ion chromatograms for 5 consecutive fractions from liver (a) and kidney (b) peptide digests are shown, indicating that proteins eluting from the C18 column at high pH and at increasing acetonitrile concentrations display different chromatographic behaviors when separated at low pH, consistent with an orthogonal fractionation strategy. Venn diagrams showing unique and shared protein components (c). Hypergeometric enrichment test for subcellular localization showed significant enrichment for proteins located in the cell membrane and extracellular matrix in both liver (d) and kidney (e). Functional enrichment analysis of shared proteome signatures is shown in (f)