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. 2015 Aug 12;5(3):1832–1854. doi: 10.3390/biom5031832

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© 2015 by the authors; licensee MDPI, Basel, Switzerland.

This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/4.0/).

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(a) Profiling of unenriched chymotryptic Asn71-glycopeptides derived from nCG in positive ionization polarity. Data points are plotted as mean ± SD, n = 3; (b) (i) CID-and (ii) ETD-MS/MS of the predominant chymotryptic GlcNAcβAsn71-glycopeptide variant (GSNINVTL); (c,d) (i) CID- and (ii) ETD-MS/MS of the chymotryptic M2F-containing N-glycopeptide originating from the interfering neutrophil proteins i.e., (c) azurocidin and (d) NE covering the N-glycosylation sites Asn126 and Asn124, respectively. See Figure S4 for glycopeptides covering other observed sites of azurocidin and NE. See also Table 1 for summary of all observed glycoforms of the three N-glycoproteins identified in the protein preparation.