Complement-component-C3-opsonized immunoglobulin G anti-DNA antibodies do not bind effectively to red blood cells unless aggregated on a high-Mr DNA matrix

Large, soluble ds (double-stranded) DNA-IgG (immunoglobulin G) anti-dsDNA immune complexes (greater than or equal to 200 S) that were previously opsonized with complement were digested with DNAase. The small complement-component-C3-fragment-labelled IgG (11-14 S) that was then isolated did not bind...

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Bibliographic Details
Published in:Biochemical journal 1984-12, Vol.224 (3), p.755-759
Main Authors: Horgan, C, Taylor, R P
Format: Article
Language:English
Subjects:
Antigen-Antibody Complex - immunology
Centrifugation, Density Gradient
Complement C3 - immunology
DNA - immunology
Erythrocytes - immunology
Humans
Immunoglobulin G - immunology
In Vitro Techniques
Molecular Weight
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Summary:Large, soluble ds (double-stranded) DNA-IgG (immunoglobulin G) anti-dsDNA immune complexes (greater than or equal to 200 S) that were previously opsonized with complement were digested with DNAase. The small complement-component-C3-fragment-labelled IgG (11-14 S) that was then isolated did not bind effectively to complement receptor type 1 on human red blood cells. However, when this IgG was immune-complexed with 3H-labelled PM2 (bacteriophage directed against a marine Pseudomonas) dsDNA (Mr approximately 6 X 10(6), substantial binding of both the DNA antigen and IgG to the erythrocytes was demonstrable.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2240755