Publikationstyp: | Beitrag in wissenschaftlicher Zeitschrift |
Art der Begutachtung: | Peer review (Publikation) |
Titel: | Oxidative tryptophan modification by terpene- and squalene-hydroperoxides and a possible link to cross-reactions in diagnostic tests |
Autor/-in: | Natsch, Andreas Emter, Roger Badertscher, Remo P. Brunner, Gerhard Granier, Thierry Kern, Susanne Ellis, Graham |
et. al: | No |
DOI: | 10.1021/acs.chemrestox.5b00039 |
Erschienen in: | Chemical Research in Toxicology |
Band(Heft): | 28 |
Heft: | 6 |
Seite(n): | 1205 |
Seiten bis: | 1208 |
Erscheinungsdatum: | 15-Jun-2015 |
Verlag / Hrsg. Institution: | American Chemical Society |
ISSN: | 0893-228X 1520-5010 |
Sprache: | Englisch |
Schlagwörter: | Hydrogen peroxide; Molecular structure; Oxidation-reduction; Tryptophan; Diagnostic test, routine |
Fachgebiet (DDC): | 540: Chemie |
Zusammenfassung: | Hydroperoxides can act as specific haptens and oxidatively modify proteins. Terpene hydroperoxides trigger unusually high frequencies of positive skin reactions in human patients if tested at high concentrations. It is unknown whether this is due to specific hapten formation. Here, we show that both terpene hydroperoxides and the endogenous hydroperoxide formed from squalene can oxidatively modify tryptophan. Oxidative modifications of Trp were recently postulated to explain cross-sensitization between unrelated photosensitizers. Current observations may extend this hypothesis: Oxidative events triggered by endogenous hydroperoxides and hydroperoxides/oxidants derived from xenobiotics might lead to a sensitized state detected by patch tests with high concentrations of hydroperoxides. |
URI: | https://digitalcollection.zhaw.ch/handle/11475/23984 |
Volltext Version: | Publizierte Version |
Lizenz (gemäss Verlagsvertrag): | Lizenz gemäss Verlagsvertrag |
Departement: | Life Sciences und Facility Management |
Organisationseinheit: | Institut für Chemie und Biotechnologie (ICBT) |
Enthalten in den Sammlungen: | Publikationen Life Sciences und Facility Management |
Dateien zu dieser Ressource:
Es gibt keine Dateien zu dieser Ressource.
Zur Langanzeige
Natsch, A., Emter, R., Badertscher, R. P., Brunner, G., Granier, T., Kern, S., & Ellis, G. (2015). Oxidative tryptophan modification by terpene- and squalene-hydroperoxides and a possible link to cross-reactions in diagnostic tests. Chemical Research in Toxicology, 28(6), 1205–1208. https://doi.org/10.1021/acs.chemrestox.5b00039
Natsch, A. et al. (2015) ‘Oxidative tryptophan modification by terpene- and squalene-hydroperoxides and a possible link to cross-reactions in diagnostic tests’, Chemical Research in Toxicology, 28(6), pp. 1205–1208. Available at: https://doi.org/10.1021/acs.chemrestox.5b00039.
A. Natsch et al., “Oxidative tryptophan modification by terpene- and squalene-hydroperoxides and a possible link to cross-reactions in diagnostic tests,” Chemical Research in Toxicology, vol. 28, no. 6, pp. 1205–1208, Jun. 2015, doi: 10.1021/acs.chemrestox.5b00039.
NATSCH, Andreas, Roger EMTER, Remo P. BADERTSCHER, Gerhard BRUNNER, Thierry GRANIER, Susanne KERN und Graham ELLIS, 2015. Oxidative tryptophan modification by terpene- and squalene-hydroperoxides and a possible link to cross-reactions in diagnostic tests. Chemical Research in Toxicology. 15 Juni 2015. Bd. 28, Nr. 6, S. 1205–1208. DOI 10.1021/acs.chemrestox.5b00039
Natsch, Andreas, Roger Emter, Remo P. Badertscher, Gerhard Brunner, Thierry Granier, Susanne Kern, and Graham Ellis. 2015. “Oxidative Tryptophan Modification by Terpene- and Squalene-Hydroperoxides and a Possible Link to Cross-Reactions in Diagnostic Tests.” Chemical Research in Toxicology 28 (6): 1205–8. https://doi.org/10.1021/acs.chemrestox.5b00039.
Natsch, Andreas, et al. “Oxidative Tryptophan Modification by Terpene- and Squalene-Hydroperoxides and a Possible Link to Cross-Reactions in Diagnostic Tests.” Chemical Research in Toxicology, vol. 28, no. 6, June 2015, pp. 1205–8, https://doi.org/10.1021/acs.chemrestox.5b00039.
Alle Ressourcen in diesem Repository sind urheberrechtlich geschützt, soweit nicht anderweitig angezeigt.