Abstract
The solubility of Cu and Zn binding proteins was studied in liver samples from clinically healthy and chronic copper poisoned sheep (CCP). Homogenized liver was divided by ultracentrifugation into cytosol and pellet. The cytosol was gelfiltrated, Cu and Zn contents were determined in the eluates as well as in the pellet. Liver homogenate, cytosol and pellet were treated with 2-mercaptoethanol (ME). The resulting clear solutions were fractionated by gel filtration followed by determination of the contents of the two metals in the eluates. In CCP sheep the solubility of Cu containing proteins from the liver homogenate and pellet increased after incubation with ME. The results suggest that in CCP sheep a considerable amount of Cu containing proteins are present in an insoluble form, which to some extent is resolubilized by ME.
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