ISSN:
1573-4986
Keywords:
bovine milk
;
lactophorin
;
proteose peptone
;
component PP3
;
O-glycan
;
ConA, concanavalin A
;
GlyCAM, glycosylation-dependent cell adhesion molecule
;
HPAE, high-pH anion-exchange, MFGM, milk fat globule membrane
;
PP, proteose peptone.
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
Abstract The heat-stable acid-soluble phosphoglycoprotein component PP3 was isolated from the bovine milk proteose peptone fraction by concanavalin A affinity chromatography. Glycopeptides from the ConA-bound fraction corresponding to the component PP3 were obtained by Pronase digestion and were separated by gel filtration into high and low-molecular-mass glycopeptides. In a previous work, we have investigated the structure of the N-glycans from the high-molecular-mass glycopeptides [Girardet et al. (1995) Eur J Biochem 234: 939–46]. Here, we describe the structure of the O-glycans from the low-molecular-mass glycopeptides. By combining methylation analysis, mass spectrometry, 400 MHz 1H-NMR spectroscopy and peptide sequence analysis, we show that the low-molecular-mass fraction contains several neutral glycopeptides. A mixture of the following three glycan structures linked to the Thr86 has been identified: GalNacα1-O-Thr, Gal(β1-3)GalNAcα1-O-Thr and Gal(β1-4)GlcNAc(β1-6)[Galβ1-3)]GalNAcα1-O-Thr. © 1998 Rapid Science Ltd
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1006973802139
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