Structural studies on oligosaccharides from mammalian glycoproteins
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 spect...
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Format: | Thesis |
Language: | English |
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1989
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author | Field, M Field, Mark Christian |
author2 | Dwek, R |
author_facet | Dwek, R Field, M Field, Mark Christian |
author_sort | Field, M |
collection | OXFORD |
description | 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 |
first_indexed | 2024-03-06T19:09:22Z |
format | Thesis |
id | oxford-uuid:163fb9d7-43b7-4347-ab81-ce3cb87cb3f9 |
institution | University of Oxford |
language | English |
last_indexed | 2024-12-09T03:31:27Z |
publishDate | 1989 |
record_format | dspace |
spelling | oxford-uuid:163fb9d7-43b7-4347-ab81-ce3cb87cb3f92024-12-01T14:48:53ZStructural studies on oligosaccharides from mammalian glycoproteinsThesishttp://purl.org/coar/resource_type/c_db06uuid:163fb9d7-43b7-4347-ab81-ce3cb87cb3f9ImmunoglobulinsNervous systemGlycoproteinsOligosaccharidesStructureSerumEnglishPolonsky Theses Digitisation Project1989Field, MField, Mark ChristianDwek, RRademacher, T 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 |
spellingShingle | Immunoglobulins Nervous system Glycoproteins Oligosaccharides Structure Serum Field, M Field, Mark Christian Structural studies on oligosaccharides from mammalian glycoproteins |
title | Structural studies on oligosaccharides from mammalian glycoproteins |
title_full | Structural studies on oligosaccharides from mammalian glycoproteins |
title_fullStr | Structural studies on oligosaccharides from mammalian glycoproteins |
title_full_unstemmed | Structural studies on oligosaccharides from mammalian glycoproteins |
title_short | Structural studies on oligosaccharides from mammalian glycoproteins |
title_sort | structural studies on oligosaccharides from mammalian glycoproteins |
topic | Immunoglobulins Nervous system Glycoproteins Oligosaccharides Structure Serum |
work_keys_str_mv | AT fieldm structuralstudiesonoligosaccharidesfrommammalianglycoproteins AT fieldmarkchristian structuralstudiesonoligosaccharidesfrommammalianglycoproteins |