Complement-mediated solubilization of immune precipitates prepared with antibodies of different avidity.
Complement-mediated solubilization of immune precipitates prepared with HSA and rat IgG anti-HSA has been quantitatively analyzed. Early and late IgG anti-HSA antibodies were obtained 27 and 49 days after immunization, respectively. Immune precipitates prepared with early IgG anti-HSA were solubilized by rat serum to a larger extent than complexes prepared with late IgG anti-HSA. The affinities for HSA of the early and late antibodies were not significantly different. The quantitative differences in solubilization were neither due to differences in the Ab/Ag ratios of the immune precipitates, nor appeared to be brought about by changes in the distribution of the antibodies over the IgG sub-classes. The avidity of the late IgG anti-HSA antibodies was higher than the avidity of the early IgG antibodies. Presumably, the avidity of the antibodies greatly affected the complement-mediated solubilization of the immune precipitates. In addition, the solubilization was found to be dependent on the conditions employed to prepare the immune precipitates.
D000818:Animals; D000915:Antibody Affinity; D000917:Antibody Formation; D011232:Chemical Precipitation; D003165:Complement System Proteins / Q000276:immunology*; D006801:Humans; D007074:Immunoglobulin G / Q000096:biosynthesis; D051381:Rats; D011917:Rats, Inbred Lew; D012709:Serum Albumin / Q000276:immunology; D012995:Solubility; D013696:Temperature; D013997:Time Factors
D007074:Immunoglobulin G; D012709:Serum Albumin; D003165:Complement System Proteins