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Title: Structural studies on oligosaccharides from mammalian glycoproteins
Author: Field, Mark C.
ISNI:       0000 0001 3463 8422
Awarding Body: University of Oxford
Current Institution: University of Oxford
Date of Award: 1989
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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.
Supervisor: Dwek, R. A. ; Rademacher, T. W. Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available
Keywords: Oligosaccharides ; Structure ; Glycoproteins ; Immunoglobulins ; Serum ; Nervous system