Isolation of immune complexes by an equine Clq-like factor.
A method for the isolation of circulating immune complexes by coprecipitation with an equine Clq-like factor is described. The Clq-like factor co-precipitated 80% of the 125I-labeled aggregated human IgG (AHG) following dialysis against 0.05 M Tris-HCl, pH 8.1 compared to only 2% of the unaggregated human IgG (HG). When incubated with bovine serum albumin (BSA) anti-BSA soluble immune complexes (IC) prepared at antigen (AG)-antibody (Ab) equivalence or in Ab excess, the Clq-like factor co-precipitated 100% of the available complexes. Under conditions of 2x Ag excess, Clq-like factor was less efficient as demonstrated by co-precipitation of 40% of the available IC. Although the nature and specificity of binding of the Clq-like factor is unknown, its isolation and partial characterization are reported.
D000818:Animals; D000936:Antigen-Antibody Complex / Q000302:isolation & purification*; D002850:Chromatography, Gel; D003172:Complement C1 / Q000276:immunology / Q000302:isolation & purification; D000939:Epitopes; D006736:Horses / Q000276:immunology; D006801:Humans; D007074:Immunoglobulin G / Q000302:isolation & purification; D007163:Immunosorbent Techniques
D000936:Antigen-Antibody Complex; D003172:Complement C1; D000939:Epitopes; D007074:Immunoglobulin G