Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase (2009)
- Authors:
- USP affiliated authors: MASCIO, PAOLO DI - IQ ; AUGUSTO, OHARA - IQ
- Unidade: IQ
- DOI: 10.1016/j.abb.2008.12.017
- Subjects: ZINCO; COBRE; SUPERÓXIDO DISMUTASE; ÓXIDO NÍTRICO; PROTEÍNAS
- Language: Inglês
- Imprenta:
- Source:
- Título do periódico: Archives of Biochemistry and Biophysics
- ISSN: 0003-9861
- Volume/Número/Paginação/Ano: v. 484, n. 2, p. 127-133, 2009
- Este periódico é de assinatura
- Este artigo NÃO é de acesso aberto
- Cor do Acesso Aberto: closed
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ABNT
VAZ, Sandra Muntz et al. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase. Archives of Biochemistry and Biophysics, v. 484, n. 2, p. 127-133, 2009Tradução . . Disponível em: https://doi.org/10.1016/j.abb.2008.12.017. Acesso em: 19 abr. 2024. -
APA
Vaz, S. M., Prado, F. M., Di Mascio, P., & Augusto, O. (2009). Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase. Archives of Biochemistry and Biophysics, 484( 2), 127-133. doi:10.1016/j.abb.2008.12.017 -
NLM
Vaz SM, Prado FM, Di Mascio P, Augusto O. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase [Internet]. Archives of Biochemistry and Biophysics. 2009 ; 484( 2): 127-133.[citado 2024 abr. 19 ] Available from: https://doi.org/10.1016/j.abb.2008.12.017 -
Vancouver
Vaz SM, Prado FM, Di Mascio P, Augusto O. Oxidation and nitration of ribonuclease and lysozyme by peroxynitrite and myeloperoxidase [Internet]. Archives of Biochemistry and Biophysics. 2009 ; 484( 2): 127-133.[citado 2024 abr. 19 ] Available from: https://doi.org/10.1016/j.abb.2008.12.017 - 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
- MS characterization of the ditryptophan cross links in lysozyme submitted to enzymatically and photolytically generated carbonate radicals
- 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
- 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
Informações sobre o DOI: 10.1016/j.abb.2008.12.017 (Fonte: oaDOI API)
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