Ion-specific electrode study of copper binding to serum albumins.
The binding of copper to bovine, human, rabbit, rat, and porcine albumin has been studied using a cupric ion-specific electrode. The results were analyzed in terms of Scatchard expression assuming two classes of independent binding sites. The high-affinity constants for copper binding to the albumin show the same trend as the first association constants for nickel binding, namely, rabbit greater than human greater than rat greater than pig. Despite the similarity in the primary amino acid sequence for human and bovine serum albumin, the former has only one high-affinity site for copper, while the latter has more than three sites.
D000818:Animals; D002417:Cattle; D003300:Copper / Q000097:blood*; D004566:Electrodes; D006801:Humans; D011485:Protein Binding; D011817:Rabbits; D051381:Rats; D012709:Serum Albumin / Q000032:analysis*; D012710:Serum Albumin, Bovine / Q000032:analysis; D013552:Swine
D012709:Serum Albumin; D012710:Serum Albumin, Bovine; D003300:Copper