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

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

Research output: Contribution to journalArticle

31 Citations (Scopus)

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 languageEnglish
Pages (from-to)593-594
Number of pages2
JournalExperientia
Volume39
Issue number6
DOIs
Publication statusPublished - Jun 1983

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styrene oxide
Oxyhemoglobins
Styrene
Erythrocytes
Oxidation
Carbon Monoxide
Hydroxyl Radical
Catalase
Superoxide Dismutase
Free Radicals
Reactive Oxygen Species

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin. / Tursi, F.; Samaia, M.; Salmona, M.; Belvedere, G.

In: Experientia, Vol. 39, No. 6, 06.1983, p. 593-594.

Research output: Contribution to journalArticle

Tursi, F. ; Samaia, M. ; Salmona, M. ; Belvedere, G. / Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin. In: Experientia. 1983 ; Vol. 39, No. 6. pp. 593-594.
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