Peroxidation of the antimalarial drug primaquine -characterization of a benzidine -like metabolite with methaemoglobin - forming activity (1993)
- Authors:
- Autor USP: AUGUSTO, OHARA - IQ
- Unidade: IQ
- DOI: 10.3109/00498259309059369
- Subjects: BIOQUÍMICA; QUÍMICA FARMACÊUTICA
- Language: Inglês
- Imprenta:
- Source:
- Título: Xenobiotica
- Volume/Número/Paginação/Ano: v.23, n.2 , p.133-9, 1993
- Este periódico é de acesso aberto
- Este artigo NÃO é de acesso aberto
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ABNT
MORAIS, M S e AUGUSTO, Ohara. Peroxidation of the antimalarial drug primaquine -characterization of a benzidine -like metabolite with methaemoglobin - forming activity. Xenobiotica, v. 23, n. 2 , p. 133-9, 1993Tradução . . Disponível em: https://doi.org/10.3109/00498259309059369. Acesso em: 20 fev. 2026. -
APA
Morais, M. S., & Augusto, O. (1993). Peroxidation of the antimalarial drug primaquine -characterization of a benzidine -like metabolite with methaemoglobin - forming activity. Xenobiotica, 23( 2 ), 133-9. doi:10.3109/00498259309059369 -
NLM
Morais MS, Augusto O. Peroxidation of the antimalarial drug primaquine -characterization of a benzidine -like metabolite with methaemoglobin - forming activity [Internet]. Xenobiotica. 1993 ;23( 2 ): 133-9.[citado 2026 fev. 20 ] Available from: https://doi.org/10.3109/00498259309059369 -
Vancouver
Morais MS, Augusto O. Peroxidation of the antimalarial drug primaquine -characterization of a benzidine -like metabolite with methaemoglobin - forming activity [Internet]. Xenobiotica. 1993 ;23( 2 ): 133-9.[citado 2026 fev. 20 ] Available from: https://doi.org/10.3109/00498259309059369 - Accumulating evidence on the contribution of free radicals in protein aggregation
- Inactivation and aggregation of protein disulfide isomerase by enzymatically and photolytically generated carbonate radical
- Spin trapping of glutathiyl and protein radicals produced from nitric oxide-derived oxidants
- Oxidants derived from the bicarbonate buffer ('HCO IND. 3'/'CO IND. 2')
- Reaction of human hemoglobin with peroxynitrite Isomerization to nitrate and secondary formation of protein radicals
- Peroxynitrite-mediated free radical formation in human plasma detected by epr
- Peroxynitrite preferentially oxidizes the dithiol redox motifs of protein disulfide isomerase
- Ditryptophan cross-links are detected in bovine beta crystallin irradiated with a solar simulator and in human lenses with advanced cataract
- Effects of some soybean flavonoids and aglycone-rich extracts in nitric oxide homeostasis
- Dna methylation by ter-butylhydroperoxide / iron ii
Informações sobre o DOI: 10.3109/00498259309059369 (Fonte: oaDOI API)
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