Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate (2004)
- Authors:
- USP affiliated authors: MASCIO, PAOLO DI - IQ ; AUGUSTO, OHARA - IQ
- Unidade: IQ
- Subjects: ÓXIDO NÍTRICO; SUPERÓXIDO DISMUTASE; PEROXIDASE
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Journal of Biological Chemistry
- ISSN: 0145-479X
- Volume/Número/Paginação/Ano: v. 279, n. 50, p. 51836-51843, 2004
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ABNT
BONINI, Marcelo Gialluisi et al. Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry, v. 279, n. 50, p. 51836-51843, 2004Tradução . . Acesso em: 19 set. 2024. -
APA
Bonini, M. G., Miyamoto, S., Di Mascio, P., & Augusto, O. (2004). Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry, 279( 50), 51836-51843. -
NLM
Bonini MG, Miyamoto S, Di Mascio P, Augusto O. Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry. 2004 ; 279( 50): 51836-51843.[citado 2024 set. 19 ] -
Vancouver
Bonini MG, Miyamoto S, Di Mascio P, Augusto O. Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate. Journal of Biological Chemistry. 2004 ; 279( 50): 51836-51843.[citado 2024 set. 19 ] - Peroxynitrite does not decompose to singlet oxygen ( `ANTPOT. delta IND. g´`O IND. 2´) and nitroxyl (N`O POT. -´)
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- 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
- MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals
- 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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