662 resultados para OXIDANT


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A rapid, templateless, surfactantless approach is proposed to prepare microfibrils by simply mixing of aqueous cupric sulfate and o-phenylenediamine (oPD) solutions at room temperature. The as-prepared poly(o-phenylenediamine) (PoPD) microfibrils have been characterized by optical microscope, transmission electron microscope (TEM), X-ray photoelectron spectroscopy (XPS), Fourier transform infrared spectroscopy (FTIR), ultraviolet-visible spectroscopy (UV-vis) and X-ray diffraction (XRD).

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Oxidative polymerization of aniline in the presence of H2O2/Fe2+/HCl was carried out, and polyaniline obtained showed similar molecular structure compared to that prepared in (NH4)(2)S2O8 system.

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To express and product a fluorescent antioxidant holo-alpha-phycocyanin (PC) of Spirulina platensis (Sp) with His-tag (rHHPC; recombinant holo-alpha-phycocyaninof Spirulina platensis with His-tag) in 5-l bench scale. A vector harbouring two cassettes was constructed: cpcA along with cpcE-cpcF in one cassette; ho1-pcyA in the other cassette. Lyases CpcE/F of Synechocystis sp. PCC6803 (S6) could catalyse the 82 site Cys in apo-alpha-PC of Sp linking with bilin chromophores, and rHHPC was biosynthesized in Escherichia coli BL21. The constant feeding mode was adopted, and transformant reached the biomass of rHHPC up to 0.55 g l(-1) broth in 5-litre bench scale. rHHPC was purified by Ni2+ affinity column conveniently. The absorbance and the fluorescence emission spectra of rHHPC had lambda(max) at 621 and 650 nm, respectively. The IC50 values of rHHPC were 277.5 +/- 25.8 mu g ml(-1) against hydroxyl radicals and 20.8 +/- 2.2 mu g ml(-1) against peroxyl radicals. Combinational biosynthesis of rHHPC was feasible, and the constant feeding mode was adopted to produce good yields of rHHPC. Fluorescent rHHPC with several unique qualitative and quantitative features was effective on scavenging hydroxyl and peroxyl radicals. A potent antioxidant rHHPC was co-expressed, produced and characterized for nutritional and pharmacological values, which would help to develop phycobiliproteins' applications in their fluorescent and biological activities.

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Propylene epoxidation by air was carried out on NaCl-modified silver (NaCl/Ag) catalysts, and the catalysts were characterized by X-ray diffraction (XRD) and X-ray photoelectron spectroscopy (XPS). The effects of NaCl loadings, propylene to oxygen ratio, and the reaction time on the catalytic performance were investigated. It was found that the addition of NaCl to silver significantly increases the propylene oxide (PO) selectivity. The PO yield has a maximum when the NaCl loading is about 10 wt.%. Also 12.4% conversion of propylene and 31.6% selectivity to PO are obtained on the NaCl/Ag (10 wt.%) catalyst at 350 degreesC, space velocity 1.8 x 10(4) h(-1) and C3H6:O-2 = 1:2. XPS and XRD characterizations show that AgCl formed on the silver catalyst was favorable to propylene epoxidation. A compound with highly oxidized Ag ion was also found, which may be effective for the reaction. (C) 2002 Elsevier Science B.V. All rights reserved.

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A bench scale reaction test for methane aromatization in the absence of an added oxidant was performed and its reaction result evaluated based on the carbon balance of the system. The result was compared with those obtained from the micro-reaction test to ensure the accuracy of the internal standard analyzing method employed in this paper. The catalytic performances of modified Mo/HZSM-5 catalysts were examined. It was found that pre-treatment by steam on HZSM-5 weakened the serious deposition of coke, and pre-impregnation of n-ethyl silicate on HZSM-5 could improve the conversion of CH4, but had little effect on coke formation. A low temperature activation procedure including pre-reduction of the catalyst with methane prevents the zeolite lattice from being seriously destroyed by high valence state Mo species when the Mo loading is high. It was suggested that Mo2C species detected by XRD spectra was the active phase for CH4 aromatization.

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Background: Chronic inhibition of nitric oxide (NO) synthesis is associated with hypertension, myocardial oxidative stress and hypertrophic remodeling. Up-regulation of the cardiomyocyte adrenomedullin (AM) / intermedin (IMD) receptor signaling cascade is also apparent in NO-deficient cardiomyocytes: augmented expression of AM and receptor activity modifying proteins RAMP2 and RAMP3 is prevented by blood pressure normalization while that of RAMP1 and intermedin (IMD) is not, indicating that the latter is regulated by a pressure-independent mechanism. Aims: to verify the ability of an anti-oxidant intervention to normalize cardiomyocyte oxidant status and to investigate the influence of such an intervention on expression of AM, IMD and their receptor components in NO-deficient cardiomyocytes. Methods: NO synthesis inhibitor, NG-nitro-L-arginine methyl ester (L-NAME, 35mg/kg/day) was given to rats for 8 weeks, with/without con-current administration of antioxidants (Vitamin C (25mg/kg/day) and Tempol (25mg/kg/day)). Results: In left ventricular cardiomyocytes isolated from L-NAME treated rats, increased oxidative stress was indicated by augmented (3.6 fold) membrane protein oxidation, enhanced expression of catalytic and regulatory subunits of pro-oxidant NADPH oxidases (NOX1, NOX2) and compensatory increases in expression of anti-oxidant glutathione peroxidase and Cu/Zn superoxide dismutases (SOD1, SOD3). Vitamin C plus Tempol did not reduce systolic blood pressure but normalized augmented plasma levels of IMD, but not of AM, and in cardiomyocytes: (i) abolished increased membrane protein oxidation; (ii) normalized augmented expression of prepro-IMD and RAMP1, but not prepro-AM, RAMP2 and RAMP3; (iii) attenuated (by 42%) increased width and normalized expression of hypertrophic markers, skeletal-�-actin and prepro-endothelin-1 similarly to blood pressure normalization but in contrast to blood pressure normalization did not attenuate augmented brain natriuretic peptide (BNP) expression. Conclusion: normalization specifically of augmented IMD/RAMP1 expression in NO-deficient cardiomyocytes by antioxidant intervention in the absence of blood pressure reduction indicates that these genes are likely to be induced directly by myocardial oxidative stress. Although oxidative stress contributed to cardiomyocyte hypertrophy, induction of IMD and RAMP1 is unlikely to be secondary to cardiomyocyte hypertrophy.