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. 2020 Mar 24;10:5317. doi: 10.1038/s41598-020-62348-6

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© The Author(s) 2020

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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Comparison of remaining ¹⁴N percentage among individual proteins in urea-soluble versus insoluble fractions. (A,B) Individual collagen and laminin proteins with their total levels (value as MS2 spectral count in parenthesis) and remaining ¹⁴N percentage (y-axis value) separately compared between their urea-soluble (open bar) and insoluble isolates (filled bar). Note that proteins in the soluble fraction had either no or less ¹⁴N proportions than their insoluble counterparts. (C) Other GBM proteins such as nidogen, perlecan and fibrillin all had the similar profile, whereas cytoskeletal actin, although more abundantly harvested in the soluble fraction (spectral count value in parenthesis), with its insoluble contents completely turned over to ¹⁵N.