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.

journal_name

Glycobiology

journal_title

Glycobiology

authors

Mechref Y,Chen P,Novotny MV

doi

10.1093/glycob/9.3.227

subject

Has Abstract

pub_date

1999-03-01 00:00:00

pages

227-34

issue

3

eissn

0959-6658

issn

1460-2423

pii

cwc019

journal_volume

9

pub_type

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