Branch specificity of purified rat liver Golgi UDP-galactose: N-acetylglucosamine beta-1,4-galactosyltransferase. Preferential transfer of of galactose on the GlcNAc beta 1,2-Man alpha 1,3-branch of a complex biantennary Asn-linked oligosaccharide.-Reference-Cited by-同舟云学术

Branch specificity of purified rat liver Golgi UDP-galactose: N-acetylglucosamine beta-1,4-galactosyltransferase. Preferential transfer of of galactose on the GlcNAc beta 1,2-Man alpha 1,3-branch of a complex biantennary Asn-linked oligosaccharide.

Published:1984-04 Issue:8 Volume:259 Page:4716-4721
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Pâquet M R,Narasimhan S,Schachter H,Moscarello M A

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference20 articles.

1. The role of alpha-lactalbumin and the A protein in lactose synthetase: a unique mechanism for the control of a biological reaction.

2. Porcine Sugar Nucleotide: Glycoprotein Glycosyltransferases. II. Blood Serum and Liver Galactosyltransferase

3. Galactosyltransferase Acceptor Specificity of the Lactose Synthetase A Protein

4. Control of glycoprotein synthesis. Lectin-resistant mutant containing only one of two distinct N-acetylglucosaminyltransferase activities present in wild type Chinese hamster ovary cells.

5. 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.

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