Skip Navigation
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Your Environment. Your Health.

Protein-derived Radicals

Free Radical Metabolism Group

Oxidative damage to tissues by hydrogen peroxide has become a recurring theme as a mechanism for the induction of a variety of medical conditions including myocardial ischemia, cancer, inflammation and aging. Proteins are a target of such damage. Most heme-containing proteins have peroxidase activity that can cause oxidative damage to a variety of biological molecules, including itself and membrane lipids. The Free Radical Metabolism Group is in the process of investigating a series of protein-derived radicals formed by myoglobin, hemoglobin and cytochrome c oxidase that utilizes the group’s new immunological-spin trapping techniques.

The group has produced polyclonal antibodies that bind specifically to the spin trap/protein adduct of 5,5-dimethyl-1-pyrroline N-oxide (DMPO). The antibodies were produced in rabbits immunized against the hapten, 5,5-dimethyl-2-octanoic acid-1-pyrroline N-oxide (OA-DMPO). OA-DMPO is a structural analog of DMPO with an additional carbon chain terminating in a carboxyl-group for amide linking. Antigens were synthesized by reacting OA-DMPO with chicken egg albumin via the carbodiimide method for amidation. Titer of the rabbit serum was determined using ELISA techniques. The polyclonal antibodies screened positive for protein-DMPO nitrone adducts produced on BSA via Fenton chemistry and adducts produced on metmyoglobin as a result of self-peroxidation by hydrogen peroxide.

Back
to Top