MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals (2014)
- Authors:
- USP affiliated authors: MASCIO, PAOLO DI - IQ ; AUGUSTO, OHARA - IQ
- Unidade: IQ
- Subjects: LISOZIMAS; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Publisher: Society for Free Radical Biology and Medicine (SFRBM)
- Publisher place: Indianápolis
- Date published: 2014
- Source:
- Título: Abstracts
- Conference titles: Annual Meeting of the Society for Free Radical Biology and Medicine (SFRBM)
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ABNT
PAVIANI, Veronica et al. MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals. 2014, Anais.. Indianápolis: Society for Free Radical Biology and Medicine (SFRBM), 2014. . Acesso em: 28 dez. 2025. -
APA
Paviani, V., Queiroz, R. F., Marquez, E. F., Di Mascio, P., & Augusto, O. (2014). MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals. In Abstracts. Indianápolis: Society for Free Radical Biology and Medicine (SFRBM). -
NLM
Paviani V, Queiroz RF, Marquez EF, Di Mascio P, Augusto O. MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals. Abstracts. 2014 ;[citado 2025 dez. 28 ] -
Vancouver
Paviani V, Queiroz RF, Marquez EF, Di Mascio P, Augusto O. MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals. Abstracts. 2014 ;[citado 2025 dez. 28 ] - Peroxynitrite does not decompose to singlet oxygen ( `ANTPOT. delta IND. g´`O IND. 2´) and nitroxyl (N`O POT. -´)
- Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase
- Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
- The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol
- Evidences for the production of the carbonate radical anion during xanthine oxidase turnover
- Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
- The carbonylation and covalent dimerization of hSOD1 caused by its bicarbonate-dependent peroxidase activity is inhibited by tempol
- Characterization of a ditryptophan cross-link in hen lysozyme oxidized by the carbonate radical
- Production of lysozyme and lysozyme-superoxide dismutase dimers bound by a ditryptophan cross-link in carbonate radical-treated lysozyme
- Organic tellurium-centered radicals evidenced by EPR spin trapping and mass spectrometry experiments: insights into the mechanism of the hydrotelluration reaction
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