Complement C1q binding affects spin-labeled heterosaccharides of rabbit antibodies in immune but not artificial immunoglobulin G aggregates.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference60 articles.
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2. Recognition of IgG by Fc receptor and complement: Effects of glycosidase digestion
3. Effects of pH treatments and deglycosylation of rabbit immunoglobulin G on the binding of C1q.
4. The use of protein A and concanavalin A to examine the possible role of the carbohydrate of IgG in the binding of Clq
5. Aglycosylantibody. Effects of exoglycosidase treatments on autochthonous antibody survival time in the circulation.
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. The Fab/c fragment of IgG produced by cleavage at cyanocysteine residues;Molecular Immunology;1991-08
2. The dynamics of glycan-protein interactions in immunoglobulins. Results of spin label studies;Glycoconjugate Journal;1990
3. Labeling of the oligosaccharide moieties of immunoglobulins;Journal of Immunological Methods;1987-05
4. Covalent attachment of sulfhydryl-specific, electron spin resonance (ESR) spin-labels to Fab' fragments of murine monoclonal antibodies that recognize human platelet membrane glycoproteins. Ddevelopment of membrane protein-specific spin probes;Biochemistry;1986-09
5. Fc:Fc interactions revealed by spin-labeled IgG heterosaccharides in model immune complexes;Biochemical and Biophysical Research Communications;1986-05
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