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Literature DB >> 1823157

Analysis of glycoprotein oligosaccharides using high-pH anion exchange chromatography.

Abstract

The natural heterogeneity of glycoprotein glycans requires that chromatography be an essential part of structural elucidation. The isomeric nature of oligosaccharide structure requires chromatography which is selective for not only composition, size and anomerity, but also ring substitutions and branching configurations. HPAEC is sensitive to these structural features and thus, has become an important new method for understanding the elusive function of glycoprotein glycans.

Entities: Chemical

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Year: 1991 PMID： 1823157 DOI： 10.1093/glycob/1.2.139

Source DB: PubMed Journal: Glycobiology ISSN： 0959-6658 Impact factor: 4.313

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Cited

13 in total

1. Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention.

Authors: S Pagny; M Cabanes-Macheteau; J W Gillikin; N Leborgne-Castel; P Lerouge; R S Boston; L Faye; V Gomord
Journal: Plant Cell Date: 2000-05 Impact factor: 11.277

2. Detection and analysis of proteins modified by O-linked N-acetylglucosamine.

Authors: Natasha E Zachara; Keith Vosseller; Gerald W Hart
Journal: Curr Protoc Protein Sci Date: 2011-11

3. Detection and analysis of proteins modified by O-linked N-acetylglucosamine.

Authors: Natasha E Zachara; Keith Vosseller; Gerald W Hart
Journal: Curr Protoc Mol Biol Date: 2011-07

4. Glycosylated equine prolactin and its carbohydrate moiety.

Authors: V Y Butnev; R R Gotschall; V L Baker; W T Moore; P W Gout; G R Bousfield
Journal: J Protein Chem Date: 1996-07

5. Separation and characterization of the two Asn-linked glycosylation sites of chicken serum riboflavin-binding protein. Glycosylation differences despite similarity of primary structure.

Authors: J S Rohrer; H B White
Journal: Biochem J Date: 1992-07-01 Impact factor: 3.857

Analysis of glycoprotein oligosaccharides using high-pH anion exchange chromatography.

1. Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention.

2. Detection and analysis of proteins modified by O-linked N-acetylglucosamine.

3. Detection and analysis of proteins modified by O-linked N-acetylglucosamine.

4. Glycosylated equine prolactin and its carbohydrate moiety.

5. Separation and characterization of the two Asn-linked glycosylation sites of chicken serum riboflavin-binding protein. Glycosylation differences despite similarity of primary structure.

Review 6. A systematic approach to protein glycosylation analysis: a path through the maze.

7. Characterization of a single glycosylated asparagine site on a glycopeptide using solid-phase Edman degradation.

Review 8. The analysis of fluorophore-labeled carbohydrates by polyacrylamide gel electrophoresis.

9. Detection and Analysis of Proteins Modified by O-Linked N-Acetylglucosamine.

Review 10. Carbohydrate analysis throughout the development of a protein therapeutic.