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 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.
Fischer
A C
AC
Department of Chemistry and Biochemistry, California State University, Fullerton 92634.
Goode
C A
CA
D000818:Animals; D002417:Cattle; D002570:Ceruloplasmin / Q000378:metabolism*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D004910:Erythrocyte Membrane / Q000378:metabolism; D004912:Erythrocytes / Q000378:metabolism*; D008970:Molecular Weight; D009571:Nitrilotriacetic Acid / Q000494:pharmacology
D002570:Ceruloplasmin; D009571:Nitrilotriacetic Acid