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Titolo:
CONCANAVALIN-A BINDING AND ENDOGLYCOSIDASE-D RESISTANCE OF BETA-1,2-XYLOSYLATED AND ALPHA-1,3-FUCOSYLATED PLANT AND INSECT OLIGOSACCHARIDES
Autore:
WILSON IBH; ALTMANN F;
Indirizzi:
UNIV DUNDEE,DEPT BIOCHEM DUNDEE DD1 4HN SCOTLAND AGR UNIV VIENNA,INST CHEM A-1190 VIENNA AUSTRIA
Titolo Testata:
Glycoconjugate journal
fascicolo: 2, volume: 15, anno: 1998,
pagine: 203 - 206
SICI:
0282-0080(1998)15:2<203:CBAERO>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
LINKED CARBOHYDRATE CHAINS; TASTE-MODIFYING PROTEIN; HORSERADISH-PEROXIDASE; N-ACETYLGLUCOSAMINE; BEAN COTYLEDONS; SUGAR CHAINS; GLYCOPEPTIDES; PHYTOHEMAGGLUTININ; GLYCOPROTEINS; LECTIN;
Keywords:
CONCANAVALIN A; ENDOGLYCOSIDASE D; PLANT OLIGOSACCHARIDES; BEE VENOM OLIGOSACCHARIDES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
26
Recensione:
Indirizzi per estratti:
Citazione:
I.B.H. Wilson e F. Altmann, "CONCANAVALIN-A BINDING AND ENDOGLYCOSIDASE-D RESISTANCE OF BETA-1,2-XYLOSYLATED AND ALPHA-1,3-FUCOSYLATED PLANT AND INSECT OLIGOSACCHARIDES", Glycoconjugate journal, 15(2), 1998, pp. 203-206

Abstract

The binding to concanavalin A (Con A) by pyridylaminated oligosaccharides derived from bromelain (Man alpha 1,6(Xyl beta 1,2) Man beta 1,4GlcNAc beta 1,4(Fuc alpha 1,3)GlcNAc), horseradish peroxidase (Man alpha 1,6(Man alpha 1,3)(Xyl beta 1,2)Man beta 1,4GlcNAc beta 1,4(Fuc alpha 1,3) GlcNAc), bee venom phospholipase A(2) (Man alpha 1,6Man beta 1,4GlcNAc beta 1,4GlcNAc and Man alpha 1,6(Man alpha 1,3)Man beta 1,4GlcNAc beta 1,4 (Fuc alpha 1,3)GlcNAc) and zucchini ascorbate oxidase (Man alpha 1,6(Man alpha 1,3)(Xyl beta 1,2)Man beta 1,4GlcNAc beta 1,4GlcNAc) was compared to the binding by Man(3)GlcNAc(2), Man(5)GlcNAc(2) and the asialo-triantennary complex oligosaccharide from bovine fetuin. While the fetuin oligosaccharide did not bind, bromelain, zucchini, Man(2)GlcNAc(2) and horseradish peroxidase were retarded (in that order). The alpha 1,3-fucosylated phospholipase, Man(3)GlcNAc(2) and Man(5)GlcNAc(2) structures were eluted with 15 mM alpha-methylmannoside. It is concluded that core alpha 1,3-fucosylation has little or no effect on ConA binding while xylosylation decreases affinity for ConA. In a parallel study comparing the endoglycosidase D (Endo D) sensitivities of Man(3)GlcNAc(2), IgG-derived GlcNAc beta 1, 2Man alpha 1,6(GlcNAc beta 1,2Man alpha 1,3)Man beta 1,4GlcNAc beta 1,4(Fuc alpha 1,6)GlcNAc, the phospholipase Man alpha 1,6(Man alpha 1,3)Man beta 1, 4GlcNAc beta1,4(Fuc alpha 1,3)GlcNAc, and horseradish and zucchini pyridylaminated N-linked oligosaccharides, it was found that only the Man(3)GlcNAc(2) structure was cleaved. The IgG structure was sensitive only when beta-hexosaminidase was also present. Thus, in contrast to core alpha 1,6-fucosylated structures, such as those present in mammals, the presence of core alpha 1,3-fucose, as found in structures from plants and insects, and/or beta 1,2-xylose, as found in plants, causes resistance toEndo D.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/07/20 alle ore 08:58:22