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. 2017 Nov 3;7:14499. doi: 10.1038/s41598-017-14833-8

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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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LC-MS analysis reveals signal peptide cleavage heterogeneity of recombinant FGF2 expressed with an amino-terminal bombyxin signal peptide. (a) The total ion chromatogram of FGF2 compared with a negative control run revealed a characteristic peak at ~7.2 min. (b) The proteomic spectrum corresponding to the peak at 7.1–7.6 min with 29 averaged scans displayed several characteristic mass-to-charge ratio peaks. (c) The transformed, deconvoluted mass spectrum of recombinant FGF2 exhibited four distinctive molecular masses, each corresponding to a different cleavage site near the junction of the bombyxin signal peptide and mature FGF2. Detected cleavage sites are indicated by red lines in the upper left sequence of the signal peptide – FGF2 junction.