Control of glycoprotein synthesis. Processing of asparagine-linked oligosaccharides by one or more rat liver Golgi alpha-D-mannosidases dependent on the prior action of UDP-N-acetylglucosamine: alpha-D-mannoside beta 2-N-acetylglucosaminyltransferase I.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference39 articles.
1. 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.
2. Chinese hamster ovary cells selected for resistance to the cytotoxicity of phytohemagglutinin are deficient in a UDP-N-acetylglucosamine--glycoprotein N-acetylglucosaminyltransferase activity.
3. Control of glycoprotein synthesis. Lectin-resistant mutant containing only one of two distinct N-acetylglucosaminyltransferase activities present in wild type Chinese hamster ovary cells.
4. Specific changes in the oligosaccharide moieties of VSV grown in different lectin-resistant CHO cells
5. Processing of high mannose oligosaccharides to form complex type oligosaccharides on the newly synthesized polypeptides of the vesicular stomatitis virus G protein and the IgG heavy chain.
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