Title : Structural characterization of the N-linked oligosaccharides in
bile salt-stimulated lipase originated from human breast milk
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
Output (sent_index, trigger,
protein,
sugar,
site):
- 1. derived, , BSSL, N- glycans, -
- 1. derived, , bile salt-stimulated lipase, N- glycans, -
- 3. monosialylated, , -, monosialylated structures, -
- 4. present, , BSSL, esterified N- glycans, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):