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- Title
The reaction between the complement subcomponent C1q, IgG complexes and polyionic molecules.
- Authors
Hughes-Jones, N. C.; Gardner, Brigitte
- Abstract
The strength of the bond between 125I-labelled Clq and immune complexes, Fc piece, dextran sulphate, polyglutamic acid and polylysine has been investigated. The binding of Clq to Fc piece, small molecular weight (< 10,000) dextran sulphate, polyglutamic acid and polylysine have values for the functional affinity constant (Ko) in the range 0.2-1.5 × 104 M-1. In contrast, the binding of Clq to immune complexes and large molecular weight polyions (> 100,000 is much greater and lies in the range 3×107 - 4×108 M-1. The differences in the binding constants between the two groups can be explained if the Fc piece and small molecular weight compounds bind to only 1 head of the Clq molecule but the immune complexes and large molecules bind to 2 heads. There are probably 6 binding sites on the Clq molecule for dextran sulphate. The enhancement of the binding affinity of Clq by reduction in ionic strength and the reaction with polyions, indicate that ionic groups are present near or within the binding sites.
- Subjects
IMMUNOGLOBULIN G; IMMUNOGLOBULINS; IMMUNE complexes; ANTIGENS; MOLECULAR weights; DEXTRAN
- Publication
Immunology, 1978, Vol 34, Issue 3, p459
- ISSN
0019-2805
- Publication type
Article