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.
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Authors | M J Elices, I J Goldstein |
Journal | The Journal of biological chemistry
(J Biol Chem)
Vol. 264
Issue 3
Pg. 1375-80
(Jan 25 1989)
ISSN: 0021-9258 [Print] United States |
PMID | 2492275
(Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)
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Chemical References |
- Oligosaccharides
- Galactosyltransferases
- N-acetyllactosamine alpha-D-galactosyltransferase
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Topics |
- Animals
- Carcinoma, Ehrlich Tumor
(enzymology)
- Chromatography, Affinity
- Chromatography, Gel
- Galactosyltransferases
(metabolism)
- Kinetics
- Oligosaccharides
(biosynthesis)
- Substrate Specificity
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