5 resultados para Plasma nitrogen doping
em BORIS: Bern Open Repository and Information System - Berna - Suiça
Resumo:
We report the synthesis and characterization of colored ZnO-based powders via solution combustion reaction of urea and zinc nitrate hexahydrate in varying molar ratios between 1:1 and 10:1. Among other techniques, we employ X-ray diffraction, nuclear magnetic resonance, and Raman spectroscopy to characterize the products. Within a narrow range of reactant ratios, we reproducibly find an unidentified, crystalline precursor phase related to isocyanuric acid next to ZnO. Finally, we complement our investigations by performing Prompt Gamma Activation Analysis (PGAA) on selected products in order to directly determine elemental bulk compositions and compare these with X-ray photoelectron spectroscopy (XPS) measurements. Our data show traces of nitrogen mainly on the surface of the particles, and thus we question the solution combustion method as a reliable synthesis toward N-doped ZnO. Furthermore, we exclude nitrogen as being responsible for the appearance of the four controversially discussed Raman bands superimposed onto the spectrum of pure ZnO (at 275, 510, 582, and 643 cm–1) and show that the combination of PGAA and XPS is an excellent and complementary method to obtain information about the distribution of the elements in question.
Resumo:
Reactive nitrogen oxide species (RNOS) have been implicated as effector molecules in inflammatory diseases. There is emerging evidence that gamma-tocopherol (gammaT), the major form of vitamin E in the North American diet, may play an important role in these diseases. GammaT scavenges RNOS such as peroxynitrite by forming a stable adduct, 5-nitro-gammaT (NGT). Here we describe a convenient HPLC method for the simultaneous determination of NGT, alphaT, and gammaT in blood plasma and other tissues. Coulometric detection of NGT separated on a deactivated reversed-phase column was linear over a wide range of concentrations and highly sensitive (approximately 10 fmol detection limit). NGT extracted from blood plasma of 15-week-old Fischer 344 rats was in the low nM range, representing approximately 4% of gammaT. Twenty-four h after intraperitoneal injection of zymosan, plasma NGT levels were 2-fold higher compared to fasted control animals when adjusted to gammaT or corrected for total neutral lipids, while alpha- and gammaT levels remained unchanged. These results demonstrate that nitration of gammaT is increased under inflammatory conditions and highlight the importance of RNOS reactions in the lipid phase. The present HPLC method should be helpful in clarifying the precise physiological role of gammaT.
Resumo:
For the efficient translocation of organic nitrogen, small peptides of two to three amino acids are posited as an important alternative to amino acids. A new transporter mediating the uptake of di- and tripeptides was isolated from Arabidopsis thaliana by heterologous complementation of a peptide transport-deficient Saccharomyces cerevisiae mutant. AtPTR1 mediated growth of S. cerevisiae cells on different di- and tripeptides and caused sensitivity to the phytotoxin phaseolotoxin. The spectrum of substrates recognized by AtPTR1 was determined in Xenopus laevis oocytes injected with AtPTR1 cRNA under voltage clamp conditions. AtPTR1 not only recognized a broad spectrum of di- and tripeptides, but also substrates lacking a peptide bond. However, amino acids, omega-amino fatty acids or peptides with more than three amino acid residues did not interact with AtPTR1. At pH 5.5 AtPTR1 had an apparent lower affinity (K-0.5 = 416 mum) for Ala-Asp compared with Ala-Ala (K-0.5 = 54 mum) and Ala-Lys (K-0.5 = 112 mum). Transient expression of AtPTR1/GFP fusion proteins in tobacco protoplasts showed that AtPTR1 is localized at the plasma membrane. In addition, transgenic plants expressing the beta-glucuronidase (uidA) gene under control of the AtPTR1 promoter demonstrated expression in the vascular tissue throughout the plant, indicative of a role in long-distance transport of di- and tripeptides.