Structural studies on oligosaccharides from mammalian glycoproteins

Thesis

A method for the purification of human serum immunoglobulin Al (IgA1), suitable for subsequent oligosaccharide analysis, was devised. The N- and 0-linked glycans of normal human serum IgA1 were released from the protein and the structures determined by a combination of gas-chromatography mass spectrometry, nuclear magnetic resonance spectroscopy and enzymatic degradation. The glycans from serum IgA1 from normal humans and patients with rheumatoid arthritis were compared. Contrary to observations for immunoglobulin G (IgG), no significant alterations in the IgA1 glycans were encountered in the disease state, suggesting that the defect is IgG specific. The antibodies HNK-1 and L2 bind to a number of glycoproteins important in neural cell adhesion and also recognise glycolipids with a sulphonylglucuronic acid residue. The saccharide from these glycolipids influences neural cell adhesion

Authors: Field, M; Field, Mark Christian

• Publication date: 1989
• DOI: 10.5287/ora-jxyvwmax5
• Type of award: DPhil
• Level of award: Doctoral
• Awarding institution: University of Oxford
• Language: English
• Subjects: Immunoglobulins; Nervous system; Glycoproteins; Oligosaccharides; Structure; Serum