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Branch specificity of bovine colostrum and calf thymus UDP-Gal: N-acetylglucosaminide beta-1,4-galactosyltransferase

The branch specificity of bovine colostrum and calf thymus UDP-Gal:N-acetylglucosaminide beta-1—-4-galactosyltransferase toward several branched oligosaccharides, which form part of the complex-type N-glycans of glycoproteins, was investigated. A novel method was used based on acetolysis of the bi[1...

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Bibliographic Details
Published in:The Journal of biological chemistry 1984-12, Vol.259 (24), p.15131-15135
Main Authors: Blanken, W M, van Vliet, A, van den Eijnden, D H
Format: Article
Language:English
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Summary:The branch specificity of bovine colostrum and calf thymus UDP-Gal:N-acetylglucosaminide beta-1—-4-galactosyltransferase toward several branched oligosaccharides, which form part of the complex-type N-glycans of glycoproteins, was investigated. A novel method was used based on acetolysis of the bi[14C,3H] galactosylated oligosaccharide products formed by the enzymes in vitro and analysis of the acetolysis fragments by high-pressure liquid chromatography. It could be established that the galactosylation of different oligosaccharide branches occurred in a preferred order. No difference in branch specificity was observed between the soluble bovine colostrum galactosyltransferase and the enzyme that had been solubilized from calf thymus membranes. A preferential pathway for the biosynthesis of bisialylated biantennary glycans is proposed.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(17)42524-5