Abstract
Oxygenated human erythrocytes catalyzed the oxidation of styrene to styrene oxide. This reaction was inhibited by CO but not by superoxide dismutase, catalase and scavengers of hydroxyl radicals. In partially deoxygenated erythrocytes styrene oxidation showed a linear relationship with the molar fraction of oxyhemoglobin. These data indicate that oxyhemoglobin and not free oxygen radicals are involved in styrene oxidation.
Original language | English |
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Pages (from-to) | 593-594 |
Number of pages | 2 |
Journal | Experientia |
Volume | 39 |
Issue number | 6 |
DOIs | |
Publication status | Published - Jun 1983 |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)