Albumin as a zinc carrier: properties of its high-affinity zinc-binding site.

@article{Lu2008AlbuminAA,
  title={Albumin as a zinc carrier: properties of its high-affinity zinc-binding site.},
  author={Jin Lu and Alan J. Stewart and Peter J. Sadler and Teresa Pinheiro and Claudia A. Blindauer},
  journal={Biochemical Society transactions},
  year={2008},
  volume={36 Pt 6},
  pages={
          1317-21
        }
}
Although details of the molecular mechanisms for the uptake of the essential nutrient zinc into the bloodstream and its subsequent delivery to zinc-requiring organs and cells are poorly understood, it is clear that in vertebrates the majority of plasma zinc (9-14 microM; approx. 75-85%) is bound to serum albumin, constituting part of the so-called exchangeable pool. The binding of metal ions to serum albumins has been the subject of decades of studies, employing a multitude of techniques, but… 

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