Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 59, Issue 8, Pages 4255-4263Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf104681p
Keywords
human milk; N-linked glycan; glycomics; prebiotics; glycobiology; glycoproteomics; glycoprotein; oligosaccharide; sialic acid; time-of-flight mass spectrometry; LC-MS
Funding
- University of California [05GEB01NHB]
- National Institute of Environmental Health Sciences (NIEHS) [P42ES004699, R01 ES002710, P42 ES011269]
- California Dairy Research Foundation
- National Science Foundation
- National Institutes of Health [2-T3-GM08799]
- Jastro Shields Research Scholarship Award
- CHARGE [P01 ES11269]
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N-Linked glycans of skim human milk proteins were determined for three mothers. N-Linked glycans are linked to immune defense, cell growth, and cell cell adhesion, but their functions in human milk are undetermined. Protein-bound N-linked glycans were released with peptidyl N-glycosidase F (PNGase SF), enriched by graphitized carbon chromatography, and analyzed with Chip-TOF MS. To be defined as N-glycans, compounds were required, in all three procedural replicates, to match, within 6 ppm, against a theoretical human N-glycan library and be at least 2-fold higher in abundance in PNGase F-treated than in control samples. Fifty-two N-linked glycan compositions were identified, and 24 were confirmed via tandem mass spectra analysis. Twenty-seven compositions have been found previously in human milk, and 25 are novel compositions. By abundance, 84% of N-glycans were fucosylated and 47% were sialylated. The majority (70%) of total N-glycan abundance was composed of N-glycans found in all three milk samples.
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