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. 2019 Mar 27;9:5243. doi: 10.1038/s41598-019-41649-5

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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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Identification and characterization of UP1 and UP2 as splicing variants of α_s2-CN by LC-MS/MS analysis. (A) Camel α_s2-CN full-length sequence is given and its coverage (81%) from peptides identified by LC-MS/MS analysis is in bold. Blue arrows indicate a cleavage of camel α_s2-CN by trypsin. Tryptic peptides indicating the presence of exon 13 and extension of exon 16 are in red. Camel α_s2-CN peptide sequences encoded by exon 13 and by the extension of exon 16 matching with Bubalus bubalis (UniProt KB accession number E9NZN2) and Sus scrofa (UniProt KB accession number P39036) are framed. The signal peptide is in italics and in grey. (B) Validation of the additional peptide sequence (AYQIIPNLR) with five and three ions from the “y” (including y7 double charged: y + + 7) and “b” series, respectively.