Abstract
Serum albumin (human, bovine) has a specific Cu(II)-ion binding site, and is proposed to act as a copper transport protein in blood plasma. Human transferrin, normally about 30% saturated with iron in vivo, has two sites/molecule capable of complexing Cu(II); one more strongly than the other (Hirose et al. 1996). The present study shows that this binding site has a slightly stronger affinity for Cu(II) than that on the albumins. However, both human- and bovine albumin could take up part of the transferrin bound Cu(II), the second order rate constant for the reaction estimated to 12 mM−1 min−1 for both species. In vivo the albumin concentration is considerably higher than that of iron-free transferrin, and it seems unlikely that the latter can compete with albumin for non-ceruloplasmin cupric ions.
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Løvstad, R.A. A kinetic study on the distribution of Cu(II)-ions between albumin and transferrin. Biometals 17, 111–113 (2004). https://doi.org/10.1023/B:BIOM.0000018362.37471.0b
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DOI: https://doi.org/10.1023/B:BIOM.0000018362.37471.0b