Production of the carbonate radical anion during xanthine oxidase turnover in the presence of bicarbonate (2004)
- Autores:
- Autores USP: MASCIO, PAOLO DI - IQ ; AUGUSTO, OHARA - IQ
- Unidade: IQ
- Assunto: BIOQUÍMICA
- Idioma: Inglês
- Imprenta:
- Fonte:
- Título do periódico: Free Radical Biology and Medicine
- ISSN: 0891-5849
- Volume/Número/Paginação/Ano: v. 37, suppl. 1, p. S25 res. 32, 2004
- Nome do evento: Annual Meeting of the Society for Free Radical Biology and Medicine
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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. Free Radical Biology and Medicine. New York: Instituto de Química, Universidade de São Paulo. . Acesso em: 24 abr. 2024. , 2004 -
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. Free Radical Biology and Medicine. New York: Instituto de Química, Universidade de São Paulo. -
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. Free Radical Biology and Medicine. 2004 ; 37 S25 res. 32.[citado 2024 abr. 24 ] -
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. Free Radical Biology and Medicine. 2004 ; 37 S25 res. 32.[citado 2024 abr. 24 ] - Evidences for the production of the carbonate radical anion during xanthine oxidase turnover
- 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
- 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
- Cytochrome c reacts with cholesterol hydroperoxides to produce lipid- and protein-derived radicals
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