Abstract
The distribution of copper in lysates prepared anaerobically from copper-resistant hepatoma cells radiolabeled with 67Cu was examined in pulse-chase experiments. Initially, the majority of the radioactivity (>85%) coeluted with copper-metallothionein. As the chase time increased there was a gradual loss of 67Cu from metallothionein, with a concomitant increase in the level of 67Cu-labeled glutathione. There was also an increase in 67Cu incorporation into superoxide dismutase. These results suggest that the chelation of copper by metallothionein from a copper-glutathione complex (Freedman, J. H., Ciriolo, M. R., and Peisach, J. (1989) J. Biol. Chem. 264, 5598–5605) is a reversible process. Further, they demonstrate that the copper bound to metallothionein is not permanently sequestered, but can be incorporated into other copper proteins.
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