Cells have evolved a variety of mechanisms to deal with elevated concentrations of essential or nonessential metal ions. Sequestration and reduced uptake and/or facilitated efflux of potentially toxic metal ions are among the most commonly used mechanisms. Prokaryotes generally limit the intraceleular concentrations of the offending ions by redued uptake or facilitated efflux. Eukarytoes detoxify heavy metal ions by sequestering the ions within stable complexs. Two families of molecules, of molecules, one represented by cysteine-rich polyeptides and the other by enzymatically sythesized glutathione or related polypeptides, are involved in the cellular sequestration of toxic metal ions. The aim of this work was to isolate, purify, and characterize a copper-binding protein (CBP) from Candida albicans. The amino-terminal sequence of the purified CBP was determined, and binding of copper was studied.
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