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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Main Authors: Field, M, Field, Mark Christian
Other Authors: Dwek, R
Format: Thesis
Language:English
Published: 1989
Subjects:
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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
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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