Wilson's Disease: Identification of an Abnormal Copper-Binding Protein

Abstract
The metal-binding protein metallothionein was isolated from the livers of Wilson's disease patients and control subjects. The metals were removed from the native protein to produce the apoprotein, and copperthionein was prepared by equilibrium dialysis. Copperthionein from Wilson's disease patients had a copper-binding constant four times as great as that of the protein from control subjects. These results suggest that the alterations in copper homeostasis in Wilson's disease result from the synthesis of an abnormal metal-binding protein with an increased affinity for copper.