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glutathione peroxidase activity in human stratum corneum: a minor transport protein distinct from the classic selenoproteins.
Stratum corneum has been shown to actively synthesize melanin, and also possesses a number of enzymatic and nonenzymatic
antioxidant defense systems. The covalent cross-linking associated with the latter isomerases the tryptophan residue of a subunit
into a cross-link product with the overall effect of increasing the functional capacity of the enzyme. These isomerases have beentermed selenoproteins because of their selenium-containing active site. We have expressed a recombinant GST fusion protein in
Escherichia coli with a proline-rich C-terminal sequence associated with cross-linking activity in human stratum corneum. This
recombinant fusion protein, designated glutathione peroxidase (GPX-His6), was purified using affinity chromatography andcharacterized by ligand blotting and protein sequencing. Whereas covalent linkage of melanocytes is an ongoing reaction inhuman stratum corneum, analogous covalent linkage in GPX-His6 is lacking in an indication that melanocytes are not present.
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