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2.
Figure 6

Figure 6. From: Coupling Mass Spectrometry-Based “Omic” Sciences with Bioguided Processing to Unravel Milk's Hidden Bioactivities.

Schematic of potential pathways to maximize the recovery of milk bioactive components.

David C Dallas, et al. J Adv Dairy Res. ;1(2):104.
3.
Figure 4

Figure 4. From: Coupling Mass Spectrometry-Based “Omic” Sciences with Bioguided Processing to Unravel Milk's Hidden Bioactivities.

Schematic of enzymatic N-glycan release from protein and workflow for characterization of the released glycans.

David C Dallas, et al. J Adv Dairy Res. ;1(2):104.
4.
Figure 5

Figure 5. From: Coupling Mass Spectrometry-Based “Omic” Sciences with Bioguided Processing to Unravel Milk's Hidden Bioactivities.

Electrophoretic gels demonstrate the sequential successful purification of target whey proteins (e.g. lactoferrin from the remaining whey proteins). Isolated fractions were analyzed on 12% SDS-PAGE after affinity chromatography.

David C Dallas, et al. J Adv Dairy Res. ;1(2):104.
5.
Figure 2

Figure 2. From: Coupling Mass Spectrometry-Based “Omic” Sciences with Bioguided Processing to Unravel Milk's Hidden Bioactivities.

Representative MALDI-MS spectra of gangliosides from bovine and human milk. Negative mode MALDI MS spectrum of (A) bovine milk gangliosides and (B) human milk gangliosides. The inserts show the structures of GM3 and GD3 gangliosides.

David C Dallas, et al. J Adv Dairy Res. ;1(2):104.
6.
Figure 3

Figure 3. From: Coupling Mass Spectrometry-Based “Omic” Sciences with Bioguided Processing to Unravel Milk's Hidden Bioactivities.

Example bioinformatic library for fucosylated BMO. Each entry includes retention time (RT), accurate mass, oligosaccharide composition (Hex (hexose-galactose in yellow and glucose in blue circles), HexNAc (N-acetylhexosamine in white squares) Fuc (fucose-red triangles), NeuAc, and NeuGc (N-glycolylneuraminic acid) and full/partial structure.

David C Dallas, et al. J Adv Dairy Res. ;1(2):104.

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