Binding of Fibronectin to Clq; Inhibition of Binding by Aggregated IgG

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Abstract
Fibronectin was shown to bind to Clq using alkaline phosphatase conjugated fibronectin and Clq coated polystyrene tubes. The binding of the alkaline phosphatase conjugated fibronectin to Clq was dose dependent and inhibited by fibronectin and by the sulfated polymers heparin and chondroitin sulfate. The fibronectin interaction was inhibited only lightly by gelatin indicating that the fibronectin-gelatin interaction was different from that with Clq. Heat aggregated IgG blocked the binding of fibronectin to Clq and fibronectin inhibited the binding of aggregated IgG to Clq. These results suggest that fibronectin may be a factor affecting the determination of immune complexes in serum specimens by Clq binding assays.