Structure of the O-glycopeptides isolated from bovine milk component PP3 |
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| Authors: | Bernadette Coddeville Jean-Michel Girardet Yves Plancke Sylvie Campagna Guy Linden Genevieve Spik |
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| Affiliation: | (1) Laboratoire de Chimie Biologique, Unite Mixte de Recherche du Centre National de la Recherche Scientifique n° 111, Universite des Sciences et Technologies de Lille, 59655 Villeneuve d!["rsquo"]("/content/p783858341100367/xlarge8217.gif") Ascq Cedex, France;(2) Laboratoire des Biosciences de lAliment, Unite Associee a lInstitut National de la Recherche Agronomique, Faculte des Sciences, Universite Henri, Poincare-Nancy 1, B.P. 239, 54506 Vandoeuvre-les-Nancy Cedex, France |
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| 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: GalNac 1-O-Thr, Gal( 1-3)GalNAc1-O-Thr and Gal(1-4)GlcNAc(1-6)[Gal1-3)]GalNAc1-O-Thr. © 1998 Rapid Science Ltd |
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| 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. |
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