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. Author manuscript; available in PMC: 2009 Mar 1.
Published in final edited form as: J Am Soc Mass Spectrom. 2007 Dec 8;19(3):428–444. doi: 10.1016/j.jasms.2007.11.022

Table 3.

Glycosylation sites and amino acid sequences of complex-type glycopeptides observed in LC-MS/MS analysis of a chymotryptic digest of reduced and alkylated E2.

Sitea Chymotryptic peptide Glycopeptide mass Glycan typec Relative abundanced

Theoretical Observed Mass accuracy
(ppm)
N41
(N423)
39HINSTAL45 1849.794 1849.786 4 Man3-GlcNAc 0.28
1995.852 1995.831 10 Man3-GlcNAc-Fuc 1
2132.873 2132.860 6 Man 6 0.80
1970.820 1970.811 4 Man 5 0.88
1808.767 1808.769 1 Man 4 0.20
1646.714 1647.711 2 Man 3 0.10
N48
(N430)
48NESLNTGWLAG58b 2198.921 2198.902 8 Man3-Fuc 0.18
2402.001 2401.984 7 Man3-GlcNAc-Fuc 1
2605.080 2605.071 4 Man3-GlcNAc2-Fuc 0.29
a

The numbers in parenthesis represent the positions of the N glycosylation sites which correspond to the positions in the HCV polyprotein of reference strain H (GenBank access number AF009606).

b

Anomalous chymotryptic cleavage sites.

c

The notation ManX indicates that X mannose residues are attached to the chitobiose core of each N-linked high mannose glycan. The rest of the notations indicate complex type glycans.

d

The relative abundance was determined from the deconvoluted mass spectrum over the mass range containing the glycopeptide ions corresponding to glycopeptides with the same amino acid sequence.