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Biosynthesis of bi-, tri-, and tetraantennary oligosaccharides containing alpha-D-galactosyl residues at their nonreducing termini. Branch specificity of the Ehrlich tumor cell alpha(1,3)-galactosyltransferase.

Abstract
The ability of Ehrlich tumor cell alpha(1,3)-galactosyltransferase to catalyze the incorporation of alpha-D-Gal residues into a specific branch of bi-, tri-, and tetraantennary oligosaccharides has been investigated by acetolysis followed by gel filtration of the fragments on Bio-Gel P-4. Taking advantage of the carbohydrate specificity of the Griffonia simplicifolia I-B4 isolectin, the mono-[14C]alpha-D-Gal derivatives were isolated by affinity chromatography. Analysis of the acetolysis fragments generated by cleavage of the multiantennary substrates indicates that the Ehrlich cell alpha(1,3)-galactosyltransferase acts preferentially on the alpha-D-Man(1,6) arm. This branch is preferred 2.5 times in bi-, 5.6-8.5 times in tri-, and 12.7 times in tetraantennary structures over the alpha-D-Man(1,3) arm. Within the alpha-D-Man(1,6) branch, in turn, there is a 1.3-1.9-fold consistently higher frequency of galactosylation of the beta-D-GlcNAc(1,2) as compared to the beta-D-GlcNAc(1,6) antenna.
AuthorsM J Elices, I J Goldstein
JournalThe Journal of biological chemistry (J Biol Chem) Vol. 264 Issue 3 Pg. 1375-80 (Jan 25 1989) ISSN: 0021-9258 [Print] United States
PMID2492275 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
Chemical References
  • Oligosaccharides
  • Galactosyltransferases
  • N-acetyllactosamine alpha-D-galactosyltransferase
Topics
  • Animals
  • Carcinoma, Ehrlich Tumor (enzymology)
  • Chromatography, Affinity
  • Chromatography, Gel
  • Galactosyltransferases (metabolism)
  • Kinetics
  • Oligosaccharides (biosynthesis)
  • Substrate Specificity

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