INTERACTION OF BOVINE CERULOPLASMIN WITH ERYTHROCYTES

Binding of ceruloplasmin to bovine erythrocytes was investigated. The interaction was specific as demonstrated by more than 85% inhibition b y excess ceruloplasmin protein. Binding was also inhibited by copper-n itrilotriacetate. The K-D for both intact erythrocytes and solubilized ghost membranes was of the order of 10(-7) M. Using an affinity colum n a specific ceruloplasmin-binding protein was isolated from ghost mem branes. The protein has an apparent molecular mass of 100,000 with sub units of 45 and 50 KDa.