Abstract
Rats and mice were injected subcutaneousty with cadmium chloride Cd 109 and zinc chloride Zn 65. Both isotopes concentrated primarily in liver and kidneys. Tissue subcellular fractionation showed 70% to 80% 109Cd and 65Zn associated with cytoplasmic soluble fraction. Soluble fraction gel filtration revealed most 109Cd was bound to proteins of 11,000 to 12,000 molecular weight; 65Zn was associated mainly with larger sized molecules. In rats, two weeks following isotope dose, depletion of 65Zn from cytoplasmic macromolecules was demonstrated; 109Cd remained fixed to cadmium-binding proteins (Cd-BP). By ion-exchange chromatography, Cd-BP was resolved into major components. Similar components were separated from human kidney Cd-BP. Presence of Cd-BP was noted in humans and monkey liver tissues. It is suggested that mammalian organism intracellular Cd-BP apparently acts as biochemical mechanism for sequestration of toxic Cd2+ ions.
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