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Glycobiology, Vol 9, 227-234, Copyright © 1999 by Oxford University Press

ORIGINAL ARTICLES

Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk

Y Mechref, P Chen and MV Novotny
Department of Chemistry, Indiana University, Bloomington, IN 47405, USA.

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.
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R. B. Trimble, C. Lubowski, C. R. Hauer III, R. Stack, L. McNaughton, T. R. Gemmill, and S. A. Kumar
Characterization of N- and O-linked glycosylation of recombinant human bile salt-stimulated lipase secreted by Pichia pastoris
Glycobiology, March 1, 2004; 14(3): 265 - 274.
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