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The autoxidation of oxyhemoglobin to methemoglobin, at pH 6.8, causes the co-oxidation of epinephrine to adrenochrome. Part of this co-oxidation was due to a hemoglobincatalyzed peroxidation of epinephrine and could be inhibited by catalase. The remainder of the co-oxidation of epinephrine was inhibited by superoxide dismutase. This indicates that the autoxidation of oxyhemoglobin results in the generation of superoxide radicals.
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Published online: November 01, 1972
Received:
May 22,
1972
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© 1972 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology.
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