A copper-binding immunoglobulin from a myeloma patient. Purification, identification, and physical characterization.

A copper.protein complex present in the serum of a hypercupremic myeloma patient has been purified to homogeneity using gel filtration, DEAE-cellulose chromatography, and concanavalin A/Sepharose affinity chromatography. Immunoelectrophoresis and hemagglutination inhibition tests showed the copper-bound protein to be an IgG1-type immunoglobulin with lambda light chains. The immunoglobulin is of normal molecular weight (150,000) with normal size light and heavy chains (28,000 and 56,000, respectively). The carbohydrate portion of the molecule appears to be abnormal in that it interacts with concanavalin A, whereas most immunoglobulins of the gammaG-type do not. The copper in the native copper.IgG complex is in an EPR-indeterminable valence state. Copper was efficiently removed from the copper.IgG complex by dialysis against 0.1 M potassium cyanide. The apo-IgG was separated from the copper.cyanide complex by gel filtration. The copper complex was reconstituted by equilibrating the apo-IgG with 7.7 muM cupric ions.