Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
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Mechref Y, Chen P, Novotny MV
Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk.
Glycobiology. 1999 Mar;9(3):227-34.
- PubMed ID
- 10024660 [ View in PubMed]
- 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.