Title : Inter-α-trypsin Inhibitor Heavy Chain H4
Abstract :
- For the protease inhibitor inter-alpha-trypsin inhibitor heavy chain H4 two O-glycosylation sites/regions, Ser640 and Thr722/723 have been described in literature (58, 65)
- In agreement with recent findings by Chandler et al., Ser640 was found to be O-glycosylated
- The O-glycopeptide 639AFPR644 (m/z 660.722+) harbors two potential O-glycosylation sites and the occupied site could be clearly inferred from the ETD spectra by the presence of a signal at m/z 490.221+, corresponding to a z+14 ion (supplemental Fig
- S5)
- In contrast to Chandler et al., but in agreement with Halim et al., ETD data of the O-glycopeptide 722QTPAPIQAPS733 (m/z 623.273+) suggested the occupancy of the sites Thr722/723 (58, 65) (supplemental Fig
- S5)
- Unfortunately, none of the two potential O-glycosylation sites could be clearly ruled out by the detected fragment ions
- Both sites/regions Ser640 and Thr722/723 were decorated with a monosialylated T-antigen
- This contrasts previous findings by Chandler et al. who also observed a disialylated T-antigen on S640
Output (sent_index, trigger,
protein,
sugar,
site):
- 2. O-glycosylated, , -, -, Ser640
- 3. O-glycopeptide, , -, -, O-glycopeptide
- 3. O-glycosylation, , -, -, sites
- 5. O-glycopeptide, , -, -, O-glycopeptide
- 5. occupancy, , -, -, sites
- 7. O-glycosylation, , -, -, sites
Output(Part-Of) (sent_index,
protein,
site):
- 1. inter-alpha-trypsin inhibitor heavy chain H4, sites/regions, Ser640
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):
- 2. inter-alpha-trypsin inhibitor heavy chain H4, -, Ser640