Abstract
Cytosols from livers of 11 freshwater fishes contain large amounts of a 10 000 Da metal-binding protein containing zinc and copper. Very little Cd accumulates in this fraction in liver after 12 months' exposure of rainbow trout to 9 μg/liter Cd in the water. Much more Cd is found in the Zn,Cu,Cd-binding protein in kidney. Characterization of the fish binding protein showed that in vitro cadmium added to cytosol displaces zinc but not copper; the ratio of sulfhydryl to Zn + Cu is 2·3–2·6; and Cu is bound in the 1 + state and is removed by bathocuproine disulfonate. By these criteria, the binding protein behaves like metallothionein.
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