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Binding Properties of the Human Complement Protein Clq

From the ¹ From the Department of Microbiology and Public Health, Michigan State University, East Lansing, Michigan, 48823

The interaction between human Clq and immunoglobulins was measured quantitatively by determining the ability of IgG, IgM, and (Fc)_5µ to inhibit the binding of ¹²⁵I-labeled Clq to IgM covalently linked to cyanogen bromide activated Sepharose. The following inhibition constants were determined: K_i for IgM = 6.42 x 10^-6 m; K_i for (Fc)_5µ = 4.35 x 10^-6 m; and K_i for IgG = 1.10 x 10^-4 m. The heat aggregation of IgM and IgG increased the ability of these proteins to bind ¹²⁵I-labeled Clq, but had no significant effect on the binding properties of (Fc)_5µ. The binding between the ¹²⁵I-labeled Clq and the IgM-Sepharose complex was inhibitable with aromatic and alkyl diamino compounds. The most potent inhibitor was 2,5-diaminotoluene.

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