RESUMO
Crystalline order of molded and then bi-axially stretched foils prepared from atactic PVC resin is investigated by means of wide-angle neutron diffraction (WAND). The observed high-resolution WAND patterns of all samples are dominated by a sharp maximum corresponding to the inter-planar distance 0.52 nm. Two weaker maxima are also resolved at 0.62 and 0.78 nm. Intensities of the peaks vary with deformation ratios of the samples and their diffraction position. Average size of the coherently scattering domains is estimated as approximately 4-8 nm. Based on the experimental data, a novel model of crystalline order of atactic PVC is proposed.
Assuntos
Cristalografia/métodos , Membranas Artificiais , Difração de Nêutrons/métodos , Cloreto de Polivinila/químicaRESUMO
The realisation of an opto-chemical ammonia sensor suitable for personal monitoring tasks is described, comprising a cyanine dye immobilised in a microporous glass thin film. The fabrication of sensor platforms incorporating embossed grating couplers provides a compact optical design with effective waveguiding characteristics, resulting in reversible ammonia sensitivity in the 5-100 ppm range in under 2 min. Cross-sensitivity of sensor response with water and other potential interferents is considered.
Assuntos
Poluição do Ar em Ambientes Fechados/análise , Amônia/análise , Monitoramento Ambiental/instrumentação , Exposição Ocupacional , Desenho de Equipamento , Humanos , Óptica e Fotônica , Sensibilidade e EspecificidadeRESUMO
We have demonstrated the presence of hydrophobic sites on the surface of Escherichia coli ribosomes by means of hydrophobic chromatography on Octyl-Sepharose. Both 30-S and 50-S ribosomal subunits adsorb to Octyl-Sepharose at a low salt concentration, and can be eluted from it with a nonionic detergent without substantial changes in structure or activity. By testing a series of LiCl-derived ribosomal cores for their ability to adsorb to Octyl-Sepharose we have shown that the interaction of ribosomal particles with Octyl-Sepharose is dependent on the presence of certain ribosomal proteins; the core particles which lack these proteins do not bind to Octyl-Sepharose. The binding of a series of different ribosomal cores to nitrocellulose filters (Millipore) yielded the same pattern as was observed with Octyl-Sepharose, i.e. the more protein-depleted the particles, the less they were adsorbed. Thus, the adsorption of ribosomes to Millipore filters and to Octyl-Sepharose is presumably of the same hydrophobic nature.
