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: 19 jan. 2026. -
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 2026 jan. 19 ] -
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 2026 jan. 19 ] - Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate
- Peroxynitrite does not decompose to singlet oxygen ( `ANTPOT. delta IND. g´`O IND. 2´) and nitroxyl (N`O POT. -´)
- 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
- Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase
- The carbonylation and covalent dimerization of human superoxide dismutase 1 caused by its bicarbonate-dependent peroxidase activity is inhibited by the radical scavenger tempol
- Linoleic acid hydroperoxide reacts with hypochlorite generating peroxyl radical intermediates and singlet oxygen
- Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen
- A comparative study of ribonuclease and lysozyme oxidation and nitration by peroxynitrite and myeloperoxidase
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