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. 2012 Jan 23;287(12):9623–9632. doi: 10.1074/jbc.M111.247874

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© 2012 by The American Society for Biochemistry and Molecular Biology, Inc.

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FIGURE 4. — Identification of O-glycopeptides of the AGP31 Pro-rich domain using MALDI-TOF MS. After separation by SDS-PAGE of an AGP31-enriched fraction obtained combining CEC and NAC, bands containing AGP31 were excised from the 50–60-kDa mass range and digested with trypsin. MALDI-TOF MS spectrum analysis showed the presence of tryptic peptides of the Pro-rich domain (P1, P2, and P4, see Figs. 1 and 3A) and associated glycopeptides, regularly spaced by 162 or 132 Da, corresponding to the mass of a hexose (gray hexagon) or a pentose (white pentagon), respectively. The numbers of hexoses and pentoses are indicated. For clarity, monoisotopic masses are indicated only for the most intense O-glycopeptides. A, MALDI-TOF MS spectrum zoom (m/z 2100–3100) on P1 and P2 O-glycopeptides. B, MALDI-TOF MS spectrum zoom (m/z 3550–4650) on P4 O-glycopeptides.