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.
Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin / F. Tursi, M. Samaja, M. Salmona, G. Belvedere. - In: EXPERIENTIA. - ISSN 0014-4754. - 39:6(1983 Jun), pp. 593-594. [10.1007/BF01971112]
Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin
M. SamajaSecondo
;
1983
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.
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