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

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Baker BL, Hultquist DE

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

J Biol Chem. 1978 Feb 25;253(4):1195-200.

PubMed ID

203585 [ View in PubMed

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Abstract

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.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Copper	Immunoglobulin lambda-like polypeptide 1	Protein	Humans	Unknown	Not Available	Details