The assembly of early components of complement on antibody-antigen aggregates and on antibody-coated erythrocytes
Autor: | J W F Goers, R R Porter |
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Rok vydání: | 1978 |
Předmět: |
Erythrocytes
Antigen-Antibody Complex Complement C3-C5 Convertases Hemolysis Biochemistry Antibodies Complement components Immunoglobulin Fab Fragments Complement C1 Molar ratio Complement Activation Molecular Biology biology Chemistry Complement C4 Complement System Proteins Cell Biology C3-convertase Complement (complexity) On cells biology.protein Antibody antigen Binding Sites Antibody Antibody Research Article |
Zdroj: | Biochemical Journal. 175:675-684 |
ISSN: | 0264-6021 |
DOI: | 10.1042/bj1750675 |
Popis: | Radioimmune assays were developed to assay the binding of complement components C1q, C1s and C4 to antibody aggregates and to cell-bound antibody. The binding of the components was compared with the haemolytic activity and with the capacity to form the C3 convertase activity in the presence of excess C2. The destruction of whole complement and of C4 activity is similar per 1,000 molecules of antibody in aggregates and cell-bound antibody, as is the binding of C1g and C1s, the latter being in a 1:2 molar ratio. The binding of C4 is about 12 times greater, per 1,000 molecules of antibody, on cells than in aggregates. However, the effective C4 molecules, as judged by the formation of C3 convertase activity, are much more similar on cells and aggregates. An assembly mechanism of the early components of complement on antibody-coated cells, which is compatible with these results, is suggested. |
Databáze: | OpenAIRE |
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