Studies on the Activation of C1 by a Univalent Hapten-Antibody Complex
| Autor: | J. Goers, B. Ziccardi, M. Glovsky, V. Schumaker |
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| Rok vydání: | 1976 |
| Předmět: | |
| Zdroj: | The Journal of Immunology. 116:1734-1735 |
| ISSN: | 1550-6606 0022-1767 |
| DOI: | 10.4049/jimmunol.116.6.1734.c |
| Popis: | The clasical serum complement system is efficiently activated by a complex formed between a monovalent DNP-polylysine hapten (nonadeca lysyl ε-DNP-lysine) and rabbit anti-DNP antibody. The hapten-antibody complex sediments as a single antibody molecule, but activates complement in the same concentration range as heat-aggregated human IgG, or immune aggregates (J. Biol. Chem. 250:4918, 1975). Activation by similar, but shorter, DNP-polylysine haptens occurs only when the polylysine chain is 9 to 10 lysyl residues in length. The activation of C1 by the hapten-antibody complex does not appear to be a result of an increased efficiency of the hapten-antibody complex to bind C1q. Ultracentrifugation studies show no difference in antibody-binding affinities to C1q with or without the DNP-polylysine hapten. However, activation of C1s to C11̄s by the hapten-antibody complex does occur at high antibody concentrations. Furthermore, the hapten-antibody complex and the hapten alone are both capable of activating a mixture of C1r and C1s. |
| Databáze: | OpenAIRE |
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