Abstract
Human milk β- N-acetylglucosaminide β1 → 4-galactosytransferase (EC 2.4.1.38) was used to galactosylate ovine submaxillary asialomucin to saturation. The major [ 14C]galactosylated product chain was obtained as a reduced oligosaccharide by β-elimination under reducing conditions. Analysis by Bio-Gel filtration and gas-liquid chromatography indicated that this compound was a tetrasaccharide composed of galactose, N-acetylglucosamine and reduced N-acetylgalactosamine in a molar ratio of 2:0.9:0.8. Periodate oxidation studies before and after mild acid hydrolysis in addition to thin-layer chromatography revealed that the most probable structure of the tetrasaccharide is Galβ1 → 3([ 14 C] Galβ1 → 4 GlcNacβ1 → 6) GalNAcol . Thus it appears that Gal β1 → 3(GlcNAc β1 → 6)GalNAc units occur as minor chains on the asialomucin. The potential interference of these chains in the assay of α- N-acetylgalactosaminylprotein β1 → 3-galactosyltransferase activity using ovine submaxillary asialomucin as an receptor can be counteracted by the addition of N-acetylglucosamine.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - General Subjects
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