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Interaction of bovine ceruloplasmin with erythrocytes
1Department of Chemistry and Biochemistry, California State University, Fullerton 92634.
Preparative Biochemistry
|May 1, 1994
Abstract:
Binding of ceruloplasmin to bovine erythrocytes was investigated. The interaction was specific as demonstrated by more than 85% inhibition by excess ceruloplasmin protein. Binding was also inhibited by copper-nitrilotriacetate. The KD for both intact erythrocytes and solubilized ghost membranes was of the order of 10(-7) M. Using an affinity column a specific ceruloplasmin-binding protein was isolated from ghost membranes. The protein has an apparent molecular mass of 100,000 with subunits of 45 and 50 KDa.