Abstract
The detailed structures of N-glycans derived from bile salt-stimulated lipase (BSSL) found in human milk were determined by combining exoglycosidase digestion with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry. The N-glycan structures were conclusively determined in terms of complexity and degree of fucosylation. Ion-exchange chromatography with pulsed amperometric detection, together with mass-spectral analysis of the esterified N-glycans, indicated the presence of monosialylated structures. The molecular mass profile of esterified N-glycans present in BSSL further permitted the more detailed studies through collision-induced dissociation (CID) and sequential exoglycosidase cleavages. The N-glycan structures were elucidated to be complex/dibranched, fucosylated/complex/dibranched, monosialylated/complex/dibranched, and monosialylated/ fucosylated/dibranched entities.
Original language | English |
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Pages (from-to) | 227-234 |
Number of pages | 8 |
Journal | Glycobiology |
Volume | 9 |
Issue number | 3 |
DOIs | |
State | Published - Mar 1999 |
Keywords
- Bile salt-stimulated lipase
- Exoglycosidases
- MALDI
- N-glycans
- TOF-MS