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. Author manuscript; available in PMC: 2014 Mar 17.
Published in final edited form as: Biochemistry. 2006 Dec 12;45(49):14755–14763. doi: 10.1021/bi0618518

Table 2.

Peptide mass mapping of the potential N-glycosylation sites in GGCX by MALDI-TOF and Q-TOF mass spectrometry

Measured m/z Measured peptide mass Expected peptide mass Corresponding residues Glycosylation site Digestions method
1821.9355a 1820.9355 1819.9911 452-466 N459 Chymotrypsin
2373.1978 2372.1978 2371.1562 458-476 N459 Trypsin
2433.2903 2432.2903 2431.2561 625-647 N627 Trypsin, Trypsin/CNBr
2617.3433 2616.3433 2615.3449 601-622 N605 Trypsin/CNBr
2646.3074 2645.3074 2644.4038 618-641 N627 Chymotrypsin
2690.4270 2689.4270 2688.3936 623-647 N627 Trypsin, Trypsin/CNBr

694.84 (2)b 1387.68 1386.68 547-559 N550 Endoproteinase Glu-C
811.71 (3) 2432.13 2431.26 625-647 N627 Trypsin, Trypsin/CNBr
897.48 (3) 2689.44 2688.39 623-647 N627 Trypsin, Trypsin/CNBr
939.44 (1) 938.44 937.44 602-609 N605 Chymotrypsin
1217.06 (2) 2432.12 2431.26 625-647 N627 Trypsin, Trypsin/CNBr
a

Top panel: deglycosylated peptide detected by MALDI-TOF MS according to the 1-Da shift theory.

b

Bottom panel: deglycosylated peptide detected by Q-TOF MS according to the 1-Da shift theory. Numbers in parentheses indicate the charges of the corresponding peptides.