A-Active Trisaccharides Isolated from A1 and A2 Blood-Group-Specific Glycoproteins

Publisher Website
Google Scholar
Abstract
Blood-group-specific glycoproteins obtained from ovarian cyst fluids of A1 and A2 persons were degraded with NaOH/NaBH4. The oligosaccharides released were de-N-acetylated with Ba(OH)2 and then hydrolyzed with dilute H2SO4. The products were fractionated on columns of ion-exchange resin and the components isolated were re-N-acetylated with 14C-labeled acetic anhydride; further purification was effected by paper chromatography. The following trisaccharides: type 1, GAlNAc(.alpha.1-3)Gal(.beta.1-3)GlcNAc; type 2, GalNAc(.alpha.1-3)-Gal(.beta.1-4)GlcNAc; type 3 (reduced), GalNAc(.alpha.1-3)Gal(.beta.1-3)GalNAcOH (where Gal is galactose, GalNAc is N-acetylgalactosamine, GlcNAc is N-acetylglucosamine and GalNAcOH is N-acetylgalactosaminitol) were isolated and characterized from both the A1 and A2 materials. The type 3 (reduced) trisaccharide has not previously been obtained from human glycoproteins. Chromatographic evidence indicated that the 3 trisaccharide structures were present in other A1, A2, A1B and A2B ovarian cyst glycoproteins and in A1 and A2 salivary glycoproteins. These findings are not indicative of structural differences between the A determinants of A1 and A2 glycoproteins.