Abstract
Zinc was able to reduce the availability of copper for several radical-generating reactions: lucigeninamplified chemiluminescence due to copper and hydrogen peroxide; copper-dependent ascorbate oxidation and its concomitant oxygen consumption: and copper-dependent benzoate hydroxylation. This was the case both in the presence of bovine serum albumin (when most zinc was protein-bound) and in its absence (when zinc was ‘available’). Competition between zinc and copper for binding to the fluorophore calcein was also examined, and this allowed assessment of copper availability in several circumstances. Competition between copper and zinc for binding to biological components seems to be a rather general phenomenon, and thus zinc is commonly a protective entity, restricting free radical generation.
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