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Catalyze free radical production

The substantia nigra and globus pallidus are rich in iron yet cerebrospinal fluid has very little iron-binding capacity (H2). Moreover, any injury to the CNS may result in the release of iron, which by Fenton/Haber-Weiss chemistry, catalyzes free radical production. Iron has also been shown to accelerate the production of CNS lipofuscin (increased in Alzheimer s disease), while various antioxidants (vitamin E, GSH, selenium) reduce its concentration (E5). [Pg.37]

The dipeptide carnosine (jS-alanyl-histidine) is able to develop antioxidative properties, at least in vitro [9]. The dipeptide, however, does not enhance the metal-catalyzed free radical production, as does histidine. The high concentrations of this metabolite enable it to act as an antioxidant and as an anti-glycox-idation compound. This makes it an interesting substance in several age-related studies [10]. [Pg.80]

Kennedy, C.H. and R.P. Mason (1990). A reexamination of the cytochrome P-450-catalyzed free radical production from a dihydropyridine. Evidence of trace transition metal catalysis. J. Biol. Chem. 265, 11425-11428. [Pg.234]

Laccase is one of the main oxidizing enzymes responsible for polyphenol degradation. It is a copper-containing polyphenoloxidase (p-diphenoloxidase, EC 1.10.3.2) that catalyzes the oxidation of several compounds such as polyphenols, methoxy-substituted phenols, diamines, and other compounds, but that does not oxidize tyrosine (Thurston, 1994). In a classical laccase reaction, a phenol undergoes a one-electron oxidation to form a free radical. In this typical reaction the active oxygen species can be transformed in a second oxidation step into a quinone that, as the free radical product, can undergo polymerization. [Pg.116]

Lipid Peroxidation and Free Radical Production Catalyzed by LOXs... [Pg.15]

LIPID PEROXIDATION AND FREE RADICAL PRODUCTION CATALYZED BY LOXs... [Pg.804]

It has been found that the 3-hydroxy-3-methylglutaryl-CoA (HMG CoA) inhibitors statins (atorvastatin, pravastatin, and cerivastatin), widely prescribed cholesterol-lowering agents, are able to inhibit phorbol ester-stimulated superoxide formation in endothelial-intact segments of the rat aorta [64] and suppress angiotensin II-mediated free radical production [65]. Delbose et al. [66] found that statins inhibited NADPH oxidase-catalyzed PMA-induced superoxide production by monocytes. It was suggested that statins can prevent or limit the involvement of superoxide in the development of atherosclerosis. It is important that statin... [Pg.920]

Alternate Crosslinking Modes. In addition to the crosslinking modes previously described, (co)polymers containing 1 and 2 may be cured by other means. For example, under appropriate acidic conditions with limited availability of active hydrogen species cyclic hemiamidals 2 will lose ROH to form the enamide 9 (Scheme 5). This has been demonstrated on model systems, e.g., 2 where vinyl is replaced by methyl ). The product, N-acetylpyrroline, has in turn been converted to nonvolatile products (oligomers) under free radical catalysis. These systems may thus be considered for application in the UV/EB or catalyzed free radical cure field. [Pg.476]

As a consequence, metal chelation is an alternative antioxidant strategy based on sequestering metal ions to prevent metal-catalyzed free radical formation [Brown et al., 1998 Guo et al., 1996 Morel et al., 1998]. To have an antioxidant action by metal chelation, a compound should be (i) able to complex the metal and yield a stable product, and (ii) the resultant complex should be a poor catalyst for the free radical generating reactions where the metal is involved. [Pg.99]

As the two one-electron redox potentials involved are close to 1V, many aromatic compounds can be oxidized to a radical cation. This is a common source of free radical production during intoxication with xenobiotics [31]. The large difference in redox potential between the two couples O2/H2O2 and H2O2/H2O provides a thermodynamic driving force for H2O2 dismutation catalyzed by catalase ... [Pg.29]


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See also in sourсe #XX -- [ Pg.438 ]




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