Abstract
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 > human > rat > 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.
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