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)

Access to Document

10.1007/BF01971112

Fingerprint Dive into the research topics of 'Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin'. Together they form a unique fingerprint.

Cite this

@article{6bf36abe97ca4987aa2828e7b7e6796b,

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",

pages = "593--594",

journal = "Cellular and Molecular Life Sciences",

issn = "1420-682X",

publisher = "Birkhauser Verlag Basel",

number = "6",

}

TY - JOUR

T1 - Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin

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.

UR - http://www.scopus.com/inward/record.url?scp=0020565231&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020565231&partnerID=8YFLogxK

U2 - 10.1007/BF01971112

DO - 10.1007/BF01971112

M3 - Article

C2 - 6852193

AN - SCOPUS:0020565231

VL - 39

SP - 593

EP - 594

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-682X

IS - 6

ER -