Abstract
The copper-containing plasma protein caeruloplasmin (Cp) has been shown to possess several oxidase activities, but with the exception of its ferrous ion oxidising (ferroxidase) activity which so far appear to be of minor biological relevance. Recently, Kim and colleagues (Kim et al. (1998) FEBS Lett. 431, pp. 473–475) observed that Cp can catalytically remove hydrogen peroxide in the presence of thiols. Here, we show that Cp can remove both hydrogen peroxide and lipid hydroperoxides at physiologically relevant concentrations of reduced glutathione known to be present in lung and lung lining fluid. The glutathione peroxidase-like activity of Cp together with its ferroxidase activity would completely remove the primary reactants required for both Fenton chemistry and lipid peroxidation.
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