Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin

F. Tursi; M. Samaia; M. Salmona; G. Belvedere

doi:10.1007/BF01971112

Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin

F. Tursi, M. Samaia, M. Salmona, G. Belvedere

Istituto di Ricerche Farmacologiche "Mario Negri"

Research output: Contribution to journal › Article › peer-review

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
Pages (from-to)	593-594
Number of pages	2
Journal	Experientia
Volume	39
Issue number	6
DOIs	https://doi.org/10.1007/BF01971112
Publication status	Published - Jun 1983

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

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10.1007/BF01971112

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title = "Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin",

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.",

author = "F. Tursi and M. Samaia and M. Salmona and G. Belvedere",

year = "1983",

month = jun,

doi = "10.1007/BF01971112",

language = "English",

volume = "39",

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journal = "Cellular and Molecular Life Sciences",

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AU - Tursi, F.

AU - Samaia, M.

AU - Salmona, M.

AU - Belvedere, G.

PY - 1983/6

Y1 - 1983/6

N2 - 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.

AB - 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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Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin

Abstract

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