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The cytosol of rabbit lung alveolar macrophages contains a high amount of peroxidase, which reduces 5-hydroperoxyeicosatetraenoic acid (5-HPETE) to 5-hydroxyeicosatetraenoic acid (5-HETE) in the presence of glutathione. This peroxidase was purified 69-fold to homogeneity with overall recovery of activity of 18.5%. The molecular mass of the enzyme was approximately 80 kDa by gel filtration, and emerged as a single band at 23.1 kDa under reducing condition by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The amino-terminal sequence of the purified peroxidase was completely identical to the sequence deduced from cellular glutathione peroxidase (cGPx) gene of rabbit liver. No other activity that reduces 5-HPETE to 5-HETE was observed during purification. These results suggest that cGPx plays an important role in metabolism of lipid hydroperoxides, especially HPETE, in lung alveolar macrophages.

Cellular Glutathione Peroxidase as a Predominant Scavenger of Hydroperoxyeicosatetraenoic Acids in Rabbit Alveolar Macrophages.