The effect of a “bisecting” N-acetylglucosaminyl group on the binding of biantennary, complex oligosaccharides to concanavalin A, Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin (RCA-12) immobilized on agarose-Reference-Cited by-同舟云学术

The effect of a “bisecting” N-acetylglucosaminyl group on the binding of biantennary, complex oligosaccharides to concanavalin A, Phaseolus vulgaris erythroagglutinin (E-PHA), and Ricinus communis agglutinin (RCA-12) immobilized on agarose

Published:1986-06 Issue:1 Volume:149 Page:65-83
ISSN:0008-6215
Container-title:Carbohydrate Research
language:en
Short-container-title:Carbohydrate Research

Author:

Narasimhan Saroja,Freed Jane C.,Schachter Harry

Publisher

Elsevier BV

Subject

Organic Chemistry,Biochemistry,General Medicine,Analytical Chemistry

Reference37 articles.

1. Control of branching during the biosynthesis of asparagine-linked oligosaccharides

2. Control of glycoprotein synthesis. UDP-GlcNAc:glycopeptide beta 4-N-acetylglucosaminyltransferase III, an enzyme in hen oviduct which adds GlcNAc in beta 1-4 linkage to the beta-linked mannose of the trimannosyl core of N-glycosyl oligosaccharides.

3. Control of glycoprotein synthesis. Bovine colostrum UDP-N-acetylglucosamine:alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine:alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase II, partial purification, and substrate specificity.

4. Control of glycoprotein synthesis.

5. Product-identification and substrate-specificity studies of the GDP-l-fucose: 2-acetamido-2-deoxy-β-d-glucoside (fuc→asn-linked GlcNAc) 6-α-l-fucosyltransferase in a golgi-rich fraction from porcine liver

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