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

Authors
  • Blanken, W M
  • van Vliet, A
  • van den Eijnden, D H
Type
Published Article
Journal
Journal of Biological Chemistry
Publisher
American Society for Biochemistry & Molecular Biology (ASBMB)
Publication Date
Dec 25, 1984
Volume
259
Issue
24
Pages
15131–15135
Identifiers
PMID: 6439717
Source
Medline
License
Unknown

Abstract

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.

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