Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin
Summary 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 m...
Ausführliche Beschreibung
Autor*in: |
Tursi, F. [verfasserIn] Samaia, M. [verfasserIn] Salmona, M. [verfasserIn] Belvedere, G. [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
1983 |
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Schlagwörter: |
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Anmerkung: |
© Birkhäuser Verlag 1983 |
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Übergeordnetes Werk: |
Enthalten in: Experientia - Birkhäuser-Verlag, 39(1983), 6 vom: 01. Juni, Seite 593-594 |
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Übergeordnetes Werk: |
volume:39 ; year:1983 ; number:6 ; day:01 ; month:06 ; pages:593-594 |
Links: |
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DOI / URN: |
10.1007/BF01971112 |
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SPR056181906 |
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10.1007/BF01971112 doi (DE-627)SPR056181906 (SPR)BF01971112-e DE-627 ger DE-627 rakwb eng Tursi, F. verfasserin aut Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin 1983 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Birkhäuser Verlag 1983 Summary 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. Oxidation (dpeaa)DE-He213 Oxygen (dpeaa)DE-He213 Hydroxyl (dpeaa)DE-He213 Superoxide (dpeaa)DE-He213 Linear Relationship (dpeaa)DE-He213 Samaia, M. verfasserin aut Salmona, M. verfasserin aut Belvedere, G. verfasserin aut Enthalten in Experientia Birkhäuser-Verlag 39(1983), 6 vom: 01. Juni, Seite 593-594 (DE-627)SPR056181736 nnns volume:39 year:1983 number:6 day:01 month:06 pages:593-594 https://dx.doi.org/10.1007/BF01971112 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_216 GBV_ILN_655 AR 39 1983 6 01 06 593-594 |
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10.1007/BF01971112 doi (DE-627)SPR056181906 (SPR)BF01971112-e DE-627 ger DE-627 rakwb eng Tursi, F. verfasserin aut Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin 1983 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Birkhäuser Verlag 1983 Summary 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. Oxidation (dpeaa)DE-He213 Oxygen (dpeaa)DE-He213 Hydroxyl (dpeaa)DE-He213 Superoxide (dpeaa)DE-He213 Linear Relationship (dpeaa)DE-He213 Samaia, M. verfasserin aut Salmona, M. verfasserin aut Belvedere, G. verfasserin aut Enthalten in Experientia Birkhäuser-Verlag 39(1983), 6 vom: 01. Juni, Seite 593-594 (DE-627)SPR056181736 nnns volume:39 year:1983 number:6 day:01 month:06 pages:593-594 https://dx.doi.org/10.1007/BF01971112 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_216 GBV_ILN_655 AR 39 1983 6 01 06 593-594 |
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10.1007/BF01971112 doi (DE-627)SPR056181906 (SPR)BF01971112-e DE-627 ger DE-627 rakwb eng Tursi, F. verfasserin aut Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin 1983 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Birkhäuser Verlag 1983 Summary 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. Oxidation (dpeaa)DE-He213 Oxygen (dpeaa)DE-He213 Hydroxyl (dpeaa)DE-He213 Superoxide (dpeaa)DE-He213 Linear Relationship (dpeaa)DE-He213 Samaia, M. verfasserin aut Salmona, M. verfasserin aut Belvedere, G. verfasserin aut Enthalten in Experientia Birkhäuser-Verlag 39(1983), 6 vom: 01. Juni, Seite 593-594 (DE-627)SPR056181736 nnns volume:39 year:1983 number:6 day:01 month:06 pages:593-594 https://dx.doi.org/10.1007/BF01971112 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_216 GBV_ILN_655 AR 39 1983 6 01 06 593-594 |
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10.1007/BF01971112 doi (DE-627)SPR056181906 (SPR)BF01971112-e DE-627 ger DE-627 rakwb eng Tursi, F. verfasserin aut Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin 1983 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Birkhäuser Verlag 1983 Summary 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. Oxidation (dpeaa)DE-He213 Oxygen (dpeaa)DE-He213 Hydroxyl (dpeaa)DE-He213 Superoxide (dpeaa)DE-He213 Linear Relationship (dpeaa)DE-He213 Samaia, M. verfasserin aut Salmona, M. verfasserin aut Belvedere, G. verfasserin aut Enthalten in Experientia Birkhäuser-Verlag 39(1983), 6 vom: 01. Juni, Seite 593-594 (DE-627)SPR056181736 nnns volume:39 year:1983 number:6 day:01 month:06 pages:593-594 https://dx.doi.org/10.1007/BF01971112 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_216 GBV_ILN_655 AR 39 1983 6 01 06 593-594 |
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10.1007/BF01971112 doi (DE-627)SPR056181906 (SPR)BF01971112-e DE-627 ger DE-627 rakwb eng Tursi, F. verfasserin aut Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin 1983 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Birkhäuser Verlag 1983 Summary 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. Oxidation (dpeaa)DE-He213 Oxygen (dpeaa)DE-He213 Hydroxyl (dpeaa)DE-He213 Superoxide (dpeaa)DE-He213 Linear Relationship (dpeaa)DE-He213 Samaia, M. verfasserin aut Salmona, M. verfasserin aut Belvedere, G. verfasserin aut Enthalten in Experientia Birkhäuser-Verlag 39(1983), 6 vom: 01. Juni, Seite 593-594 (DE-627)SPR056181736 nnns volume:39 year:1983 number:6 day:01 month:06 pages:593-594 https://dx.doi.org/10.1007/BF01971112 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_22 GBV_ILN_24 GBV_ILN_31 GBV_ILN_216 GBV_ILN_655 AR 39 1983 6 01 06 593-594 |
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Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin Oxidation (dpeaa)DE-He213 Oxygen (dpeaa)DE-He213 Hydroxyl (dpeaa)DE-He213 Superoxide (dpeaa)DE-He213 Linear Relationship (dpeaa)DE-He213 |
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styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin |
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Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin |
abstract |
Summary 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. © Birkhäuser Verlag 1983 |
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Summary 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. © Birkhäuser Verlag 1983 |
abstract_unstemmed |
Summary 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. © Birkhäuser Verlag 1983 |
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Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR056181906</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20240611064704.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">240611s1983 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/BF01971112</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR056181906</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)BF01971112-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Tursi, F.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Styrene oxidation to styrene oxide in human erythrocytes is catalyzed by oxyhemoglobin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1983</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Birkhäuser Verlag 1983</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Summary 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.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Oxidation</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Oxygen</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Hydroxyl</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Superoxide</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Linear Relationship</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Samaia, M.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Salmona, M.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Belvedere, G.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Experientia</subfield><subfield code="d">Birkhäuser-Verlag</subfield><subfield code="g">39(1983), 6 vom: 01. Juni, Seite 593-594</subfield><subfield code="w">(DE-627)SPR056181736</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:39</subfield><subfield code="g">year:1983</subfield><subfield code="g">number:6</subfield><subfield code="g">day:01</subfield><subfield code="g">month:06</subfield><subfield code="g">pages:593-594</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">https://dx.doi.org/10.1007/BF01971112</subfield><subfield code="m">X:SPRINGER</subfield><subfield code="x">Resolving-System</subfield><subfield code="z">lizenzpflichtig</subfield><subfield code="3">Volltext</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">SYSFLAG_0</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_SPRINGER</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_22</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_24</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_31</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_216</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_ILN_655</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">39</subfield><subfield code="j">1983</subfield><subfield code="e">6</subfield><subfield code="b">01</subfield><subfield code="c">06</subfield><subfield code="h">593-594</subfield></datafield></record></collection>
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