Evidences for the production of the carbonate radical anion during xanthine oxidase turnover (2003)
- Authors:
- USP affiliated authors: MASCIO, PAOLO DI - IQ ; AUGUSTO, OHARA - IQ
- Unidade: IQ
- Subjects: BIOQUÍMICA; RADICAIS LIVRES
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Programa e Resumos
- Conference titles: Reunião Anual da Sociedade Brasileira de Bioquímica e Biologia Molecular
-
ABNT
BONINI, Marcelo Gialluisi et al. Evidences for the production of the carbonate radical anion during xanthine oxidase turnover. 2003, Anais.. São Paulo: SBBq, 2003. . Acesso em: 24 abr. 2024. -
APA
Bonini, M. G., Miyamoto, S., Di Mascio, P., & Augusto, O. (2003). Evidences for the production of the carbonate radical anion during xanthine oxidase turnover. In Programa e Resumos. São Paulo: SBBq. -
NLM
Bonini MG, Miyamoto S, Di Mascio P, Augusto O. Evidences for the production of the carbonate radical anion during xanthine oxidase turnover. Programa e Resumos. 2003 ;[citado 2024 abr. 24 ] -
Vancouver
Bonini MG, Miyamoto S, Di Mascio P, Augusto O. Evidences for the production of the carbonate radical anion during xanthine oxidase turnover. Programa e Resumos. 2003 ;[citado 2024 abr. 24 ] - 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
- MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals
- 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
- Human cataracts contain cross-links produced from crystallin-derived tryptophanyl and tyrosyl radicals
- 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
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