| Literature DB >> 5430788 |
N E Hyslop, R R Dourmashkin, N M Green, R R Porter.
Abstract
Hapten-antibody complexes prepared at equivalence with the bivalent hapten bis-DNP-octamethylene-diamine and purified rabbit anti-DNP antibody were fractionated by Sepharose gel-filtration and the fractions examined by electron microscopy. Individual fractions were tested for whole-complement fixation and C1 fixation. Dimer forms did not show this type of biological activity, while fractions containing tetramers and larger polymers exhibited both C and C1 fixation, which could be inhibited by prior exposure of the complexes to the univalent hapten epsilon-DNP-caproic acid. The dose-response result indicated that the C-fixation observed was not due to interpolymeric cooperative effects. It was concluded that in the generation of biological activity by soluble antigen-antibody complexes made with complement-fixing antibody, quaternary structural changes following specific combination with antigen may be as important as any tertiary structural alterations that occur in the individual immunoglobulin molecule.Entities:
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Year: 1970 PMID: 5430788 PMCID: PMC2138777 DOI: 10.1084/jem.131.4.783
Source DB: PubMed Journal: J Exp Med ISSN: 0022-1007 Impact factor: 14.307