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Titolo:
Structural analysis of trisialylated biantennary glycans isolated from mouse serum transferrin - Characterization of the sequence Neu5Gc(alpha 2-3)Gal(beta 1-3)[Neu5Gc(alpha 2-6)]GlcNAc(beta 1-2)Man
Autore:
Coddeville, B; Regoeczi, E; Strecker, G; Plancke, Y; Spik, G;
Indirizzi:
Univ Sci & Technol Lille, Chim Biol Lab, CNRS, UMR 8576, F-59655 Villeneuve Dascq, France Univ Sci & Technol Lille Villeneuve Dascq France F-59655 e Dascq, France McMaster Univ, Hlth Sci Ctr, Dept Pathol, Hamilton, ON L8N 3Z5, Canada McMaster Univ Hamilton ON Canada L8N 3Z5 ol, Hamilton, ON L8N 3Z5, Canada
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-GENERAL SUBJECTS
fascicolo: 3, volume: 1475, anno: 2000,
pagine: 321 - 328
SICI:
0304-4165(20000726)1475:3<321:SAOTBG>2.0.ZU;2-O
Fonte:
ISI
Lingua:
ENG
Soggetto:
GAS-LIQUID-CHROMATOGRAPHY; N-GLYCOLYLNEURAMINIC ACID; HUMAN SEROTRANSFERRIN; CARBOHYDRATE MOIETY; MASS-SPECTROMETRY; METHYL GLYCOSIDES; RAT-LIVER; GLYCOPROTEINS; IDENTIFICATION; PROTEINS;
Keywords:
transferrin; glycoprotein; N-glycolylneuraminic acid; sialyltransferase ST6GlcNAc; mouse;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
39
Recensione:
Indirizzi per estratti:
Indirizzo: Spik, G Univ Sci & Technol Lille, Chim Biol Lab, CNRS, UMR 8576, F-59655 Villeneuve Dascq, France Univ Sci & Technol Lille Villeneuve Dascq France F-59655 France
Citazione:
B. Coddeville et al., "Structural analysis of trisialylated biantennary glycans isolated from mouse serum transferrin - Characterization of the sequence Neu5Gc(alpha 2-3)Gal(beta 1-3)[Neu5Gc(alpha 2-6)]GlcNAc(beta 1-2)Man", BBA-GEN SUB, 1475(3), 2000, pp. 321-328

Abstract

Five variants of mouse serum transferrin (mTf, designated mTf-I to mTf-V) with respect to carbohydrate composition have been isolated by DEAE-cellulose chromatography in the following relative percentages: mTf-I: 0.55; mTf-II: 0.79; mTf-III: 71.80; mTf-VI: 21.90 and mTf-V: 4.96, The primary structures of the major glycans from mTf-III and mTf-IV were determined by methylation analysis and H-1-nuclear magnetic resonance (NMR) spectroscopy. All glycans possessed a common trimannosyl-N,N'-diacetylchitobiose core. From theglycovariant mTf-III two isomers of a conventional biantennary N-acetyllactosamine type were isolated, in which two N-glycolylneuraminic acid (Neu5Gc) residues are linked to galactose either by a (alpha 2-6) or (alpha 2-3) linkage. A subpopulation of this glycovariant contains a fucose residue (alpha 1-6)-linked to GlcNAc-1. The structure of the major glycan found in variant mTf-IV contained an additional Neu5Gc and possessed the following new type of linkage: Neu5Gc(alpha 2-3)Gal(beta 1-3)[Neu5Gc(alpha 2-6)]GlcNAc(beta 1-2)Man(alpha 1-3). In addition to this glycan, a minor compound contained the same antennae linked to Man(alpha 1-6). In fraction mTf-V, which was found to be very heterogeneous by H-1 NMR analysis, carbohydrate composition and methylation analysis suggested the presence of tri'-antennary glycanssialylated by Neu5Gc alpha-2,6- and alpha-2,3-linked to the terminal galactose residues. In summary, mTf glycans differed from those of other analyzed mammalian transferrins by the presence of Neu5Gc and by a Neu5Gc(alpha 2-6)GlcNAc linkage in trisialylated biantennary structures, reflecting in mouse liver, a high activity of CMP-Neu5Ac hydroxylase and (alpha 2-6)GlcNAc sialyltransferase. (C) 2000 Elsevier Science B.V. All rights reserved.

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Documento generato il 15/07/20 alle ore 08:19:11