Macromolecular ligands of exchangeable copper, zinc and cadmium in human serum

✍ Scribed by Eugene L. Giroux; Robert I. Henkin

• Publisher: Elsevier Science
• Year: 1973
• Weight: 463 KB
• Volume: 2
• Category: Article
• ISSN: 0006-3061
• DOI: 10.1016/s0006-3061(00)80156-8

✦ Synopsis

Dissociation of metal-protein complexes of copper, zinc, and cadmium in human serum by histidine and glycine was studied. Distribution of metal between protein-complexed and amino acid-complexed species as a function of amino acid concentration is similar for solutions of human serum albumin and native human serum, indicating that human serum albumin and the macromolecular ligands which complex loosely bound sermn copper, zinc, and cadmium have equal avidity for these metal ions. Copperalbumin complex is the least stable, cadmium-albumin complex the most stable, with respect to dissociation by histidine.