The action of hydrogen peroxide on soluble proteins of the rat cornea has been evaluated. Two major corneal proteins are found to be oxidized by 10 mM hydrogen peroxide. Protein sequence and antibody recognition has shown one of the proteins to be albumin. Treatment of pure rat or human albumin with hydrogen peroxide oxidizes the protein and decreases its affinity for its antibody. Because albumin is a major protein in the cornea, its ready oxidation suggests that a role for albumin in this tissue may be to act as a native antioxidant, scavenging hydrogen peroxide and thus preventing more extensive damage by this toxin. These data are relevant to the evaluation of the safety of contact lens disinfectants containing hydrogen peroxide and suggest that further study of the action of this oxidant is warranted.
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