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The reactivity of oytho-methoxy-substituted catechol radicals with sulfhydryl groups: Contribution for the comprehension of the mechanism of inhibition of NADPH oxidase by apocynin
(Elsevier B.V., 2007-08-01)
Redox processes are involved in the mechanism of action of NADPH oxidase inhibitors such as diphenyleneiodonium and apocynin. Here, we studied the structure-activity relationship for apocynin and analogous ortho-methoxy- ...
The reactivity of oytho-methoxy-substituted catechol radicals with sulfhydryl groups: Contribution for the comprehension of the mechanism of inhibition of NADPH oxidase by apocynin
(Elsevier B.V., 2007-08-01)
Redox processes are involved in the mechanism of action of NADPH oxidase inhibitors such as diphenyleneiodonium and apocynin. Here, we studied the structure-activity relationship for apocynin and analogous ortho-methoxy- ...
Reactions of Nifurtimox with critical sulfhydryl-containing biomolecules: Their potential toxicology relevance
(John Wiley & Sons Ltd, 2004-05)
Nifurtimox (Nfx) is a drug used in the treatment of Chagas' disease, an endemic parasitic disease from Latin American countries. It produces undesirable side-effects in patients, frequently forcing the treatment to be ...
Purification, partial kinetic characterization and reactive sulfhydryl groups of the phosphoenolpyruvate carboxykinase from Perumytilus purpuratus adductor muscle
(1995)
Phosphoenolpyruvate carboxykinase (PEPCK) from the adductor muscle of Perumytilus purpuratus was purified to homogeneity, as determined by SDS-polyacrylamide gel electrophoresis (PAGE). The purification consisted of a ...
Inhibition of mitochondrial permeability transition by low pH is associated with less extensive membrane protein thiol oxidation
(Kluwer Academic/plenum PublNew YorkEUA, 1999)
Effect of high hydrostatic pressure on free sulfhydryl content fromfungal α-amylaseEfecto de la alta presión hidrostática en la exposición del contenido de sulfhidrilos libres en amilasa fúngica
(Laboratorio Tecnológico del Uruguay - LATU, 2018)
The Cysteine-Rich Protein Thimet Oligopeptidase as a Model of the Structural Requirements for S-glutathiolation and Oxidative Oligomerization
(PUBLIC LIBRARY SCIENCESAN FRANCISCO, 2012)
Thimet oligopeptidase (EP24.15) is a cysteine-rich metallopeptidase containing fifteen Cys residues and no intra-protein disulfide bonds. Previous work on this enzyme revealed that the oxidative oligomerization of EP24.15 ...