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1.
Figure 3

Figure 3. From: Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.

SSG Map of O-Glycoproteins. SSG of a mixture of proteins extracted from vLDL nanoparticles for two O-glycoproteins. a. APOC3 b. APOE. Yellow squares: HexNAc, Yellow circles: Hex, Purple diamonds: NeuAc. Red triangles: dHex.

John S. Strum, et al. Anal Chem. ;85(12):5666-5675.

CitationFull text

2.
Figure 4

Figure 4. From: Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.

Separation of Glycopeptides. On-line separation and detection of glycopeptides from human lactoferrin and polymeric immunoglobulin receptor, two glycoproteins isolated in a gel band after SDS-PAGE of raw human milk.

John S. Strum, et al. Anal Chem. ;85(12):5666-5675.

CitationFull text

3.
Figure 1

Figure 1. From: Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.

TDA Compliance. Score distributions of the target and decoy N-glycopeptide matches from the mixture of bovine fetuin, lactoferrin, and kappa casein. Data includes both 20 and 40% ACN SPE fractions. a. Without self-consistency. b. With self-consistency. c. With self-consistency and TDA-compliance.

John S. Strum, et al. Anal Chem. ;85(12):5666-5675.

CitationFull text

4.
Figure 2

Figure 2. From: Automated assignments of N- and O-site specific glycosylation with extensive glycan heterogeneity of glycoprotein mixtures.

Self-consistent Data. Tandem mass spectra of site-specific N-glycopeptide analysis at site 495 of bovine lactoferrin showing putative glycan structures. Glycan self-consistency is shown in a (m/z 1068.9363) and b (m/z 1089.9696). Peptide self-consistency is shown in b and c (m/z 988.4189). Blue squares: HexNAc, Gray circles: Hex, Green circles: Man. * Denotes precursor.

John S. Strum, et al. Anal Chem. ;85(12):5666-5675.

CitationFull text

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