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dc.contributor.author
Diaz Gomez, Maria Isabel
dc.contributor.author
Castro, Gerardo Daniel
dc.contributor.author
Delgado de Layo, A. M. A.
dc.contributor.author
Costantini, Martin Hernan
dc.contributor.author
Castro, Jose Alberto
dc.date.available
2019-03-14T19:04:11Z
dc.date.issued
2000-11
dc.identifier.citation
Diaz Gomez, Maria Isabel; Castro, Gerardo Daniel; Delgado de Layo, A. M. A.; Costantini, Martin Hernan; Castro, Jose Alberto; Cytochrome P450 reductase-mediated anaerobic biotransformation of ethanol to 1-hydroxyethyl-free radicals and acetaldehyde; Elsevier Ireland; Toxicology; 154; 1-3; 11-2000; 113-122
dc.identifier.issn
0300-483X
dc.identifier.uri
http://hdl.handle.net/11336/71677
dc.description.abstract
The ability of cytochrome P450 reductase to metabolize ethanol (EtOH) to acetaldehyde (AC) and 1-hydroxyethyl free radicals (1HEt) in anaerobic media was studied. Determination of AC was made by GC-FID analysis of the head space of incubation mixtures. The formation of 1HEt was established by GC-MS analysis of the adduct formed between the radical and the spin trap PBN. Results showed that pure human P450 reductase is able to biotransform EtOH to AC and 1HEt in a NADPH-dependent process under an oxygen-free nitrogen atmosphere. Pure FAD in the presence of NADPH was also able to generate AC and 1HEt from the alcohol. Anaerobic incubation mixtures containing either rat liver microsomes or pure nuclei were also able to biotransform EtOH to AC and 1HEt in the presence of NADPH. These processes were inhibited by antibody against rat liver microsomal P450 reductase. Results suggest that semiquinone forms of the flavin in P450 reductase may biotransform EtOH. These reactions might be of some significance in tissues where the P450 reductase is present in the absence of specific forms of cytochrome P450 known to be involved in EtOH metabolism (e.g. CYP2E1). However the toxicological significance of this enzymatic process remains to be established.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Ireland
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
1-Hydroxyethyl Free Radical
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Acetaldehyde
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Anaerobic Biotransformation
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Cytochrome P450 Reductase
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Ethanol
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Otras Ciencias Biológicas
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Cytochrome P450 reductase-mediated anaerobic biotransformation of ethanol to 1-hydroxyethyl-free radicals and acetaldehyde
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-03-14T14:12:29Z
dc.journal.volume
154
dc.journal.number
1-3
dc.journal.pagination
113-122
dc.journal.pais
Irlanda
dc.journal.ciudad
Shannon
dc.description.fil
Fil: Diaz Gomez, Maria Isabel. Consejo Nacional de Investigaciones Científicas y Técnicas. GP. CITEFA - Centro de Investigaciones Toxicológicas (I); Argentina
dc.description.fil
Fil: Castro, Gerardo Daniel. Consejo Nacional de Investigaciones Científicas y Técnicas. Unidad de Investigación y Desarrollo Estratégico para la Defensa. Ministerio de Defensa. Unidad de Investigación y Desarrollo Estratégico para la Defensa; Argentina
dc.description.fil
Fil: Delgado de Layo, A. M. A.. Consejo Nacional de Investigaciones Científicas y Técnicas. GP. CITEFA - Centro de Investigaciones Toxicológicas (I); Argentina
dc.description.fil
Fil: Costantini, Martin Hernan. Consejo Nacional de Investigaciones Científicas y Técnicas. GP. CITEFA - Centro de Investigaciones Toxicológicas (I); Argentina
dc.description.fil
Fil: Castro, Jose Alberto. Consejo Nacional de Investigaciones Científicas y Técnicas. Unidad de Investigación y Desarrollo Estratégico para la Defensa. Ministerio de Defensa. Unidad de Investigación y Desarrollo Estratégico para la Defensa; Argentina
dc.journal.title
Toxicology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/S0300-483X(00)00325-5
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0300483X00003255
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