Analysis of Water Surface Osccilation at Open-Channel Side Cavity by Image Analysys and Large Eddy Simulation

Source: ICHE Conference Archive - https://mdi-de.baw.de/icheArchiv

Performance of a carbon monoxide sensor based on zirconia-doped ceria

AbstractResistive-type carbon monoxide sensors were fabricated using zirconia-doped ceria, and their sensing properties were evaluated and compared with equivalent devices based on non-doped ceria. The response of both sensor types was found to increase with decreasing temperature, while the response at 450°C of a sensor fired at 950°C was greater than that of a sensor fired at 1100°C. When fired at 950°C, however, the response at 450°C of a sensor created using zirconia-doped ceria was slightly less than that of a sensor constructed from non-doped ceria. Multivariate analysis confirmed that the response of both sensor types is proportional to the resistance raised to the power of about 0.5, and inversely proportional to the particle size raised to a power of about 0.8. The sensor response time can be considered almost the same regardless of whether zirconia doping is used or not

Resistive Oxygen Sensor Using Ceria-Zirconia Sensor Material and Ceria-Yttria Temperature Compensating Material for Lean-Burn Engine

Temperature compensating materials were investigated for a resistive oxygen sensor using Ce0.9Zr0.1O2 as a sensor material for lean-burn engines. The temperature dependence of a temperature compensating material should be the same as the sensor material; therefore, the Y concentration in CeO2-Y2O3 was optimized. The resistance of Ce0.5Y0.5O2-δ was independent of the air-to-fuel ratio (oxygen partial pressure), so that it was confirmed to function as a temperature compensating material. Sensor elements comprised of Ce0.9Zr0.1O2 and Ce0.5Y0.5O2-δ were fabricated and the output was determined to be approximately independent of the temperature in the wide range from 773 to 1,073 K

Renaturation of the mature subtilisin BPN' immobilized on agarose beads

AbstractWe report here another example of renaturation of subtilisin BPN′(Sbtl) by using an immobilized preparation instead of applying a digestible mutant of Streptomyces subtilisin inhibitor (SSI), a proteinaceous inhibitor of Sbtl [M. Matsubara et al. (1994) FEBS Letters 342, 193–196]. The mature Sbtl was immobilized on agarose beads employing the amino group of the protein. After thorough washing, the immobilized Sbtl was subjected to denaturation in 6 M guanidine hydrochloride (GdnHCl) at pH 2.4 for 4 h, followed by renaturation in 2 M potassium acetate at pH 6.5 for 24 h. This denaturation/renaturation cycle was repeated five times. The recovered activity of the renatured immobilized Sbtl settled at a constant level after the third denaturation/renaturation cycle, demonstrating that almost 100% renaturation was attained by use of the immobilized Sbtl. This immobilized Sbtl preparation could well be utilized for the mechanistic study of protein folding. We then found that 2 M potassium acetate was superior to 2 M potassium chloride as a refolding medium and that the ability of SSI to induce the correct shape of the mature Sbtl was lacking in several refolding media in both thermodynamic and kinetic criteria. Thus the main cause for the increase of refolding yield of Sbtl by coexistence of SSI was prevention of the autolysis of Sbtl

Effects of High-Humidity Aging on Platinum, Palladium, and Gold Loaded Tin Oxide—Volatile Organic Compound Sensors

This study is an investigation of high-humidity aging effects on the total volatile organic compound (T–VOC) gas-sensing properties of platinum, palladium, and gold-loaded tin oxide (Pt,Pd,Au/SnO2) thick films. The sensor responses of the high-humidity aged Pt,Pd,Au/SnO2, a non-aged Pt,Pd,Au/SnO2, and a high-humidity aged Pt/SnO2 to T–VOC test gas have been measured. The high-humidity aging is an effective treatment for resistance to humidity change for the Pt,Pd,Au/SnO2 but not effective for the Pt/SnO2. The mechanism of the high-humidity aging effects is discussed based on the change of surface state of the SnO2 particles

Copy number loss of (src homology 2 domain containing)-transforming protein 2 (SHC2) gene: discordant loss in monozygotic twins and frequent loss in patients with multiple system atrophy

<p>Abstract</p> <p>Background</p> <p>Multiple system atrophy (MSA) is a sporadic disease. Its pathogenesis may involve multiple genetic and nongenetic factors, but its etiology remains largely unknown. We hypothesized that the genome of a patient with MSA would demonstrate copy number variations (CNVs) in the genes or genomic regions of interest. To identify genomic alterations increasing the risk for MSA, we examined a pair of monozygotic (MZ) twins discordant for the MSA phenotype and 32 patients with MSA.</p> <p>Results</p> <p>By whole-genome CNV analysis using a combination of CNV beadchip and comparative genomic hybridization (CGH)-based CNV microarrays followed by region-targeting, high-density, custom-made oligonucleotide tiling microarray analysis, we identified disease-specific copy number loss of the (Src homology 2 domain containing)-transforming protein 2 (<it>SHC2</it>) gene in the distal 350-kb subtelomeric region of 19p13.3 in the affected MZ twin and 10 of the 31 patients with MSA but not in 2 independent control populations (<it>p </it>= 1.04 × 10^-8, odds ratio = 89.8, Pearson's chi-square test).</p> <p>Conclusions</p> <p>Copy number loss of <it>SHC2 </it>strongly indicates a causal link to MSA. CNV analysis of phenotypically discordant MZ twins is a powerful tool for identifying disease-predisposing loci. Our results would enable the identification of novel diagnostic measure, therapeutic targets and better understanding of the etiology of MSA.</p

Basement Membrane beneath Serous Mesothelial Cells Contains α1(IV), α2(IV), α5(IV), and α6(IV) Chains of Type IV Collagen Demonstrated by Chain-specific Monoclonal Antibodies

Serous membrane (SM) covers inner surface of abdominal, thoracic and pericardial cavities, aswell as outer surface of organs inside the cavities. It consists of surface mesothelial cells andloose connective tissue. Between them, a thim layer of basement membrane (BM) is located. Type IVcollagen is major constituent of BM, and consists of 6 different a(IV) chains, a1(IV) through a6(IV).Chain-specific functions are assumed by a chain-specific manner of localization. The a(IV) chaincomposition of skin, covering outer surface of the body, is demonstrated to have a1(IV), a2(IV), a5(IV),and a6(IV) chains, whereas that of SM, covering inner surface of the body, is yet to be analyzed. Abdominal wall, small intestine, thoracic wall, lung, pericardium and epicardium of humanmaterials were used in this study. Chain-specific monoclonal antibodies (mAbs) used were H11(for a1), H22 (for a2), H31 (fo a3), H43 (for a4), H53 (for a5) and H63 (for a6). Fresh frozen sectionswere stained with indirect immunofluorescence staining using the mAbs. Four out of six a(IV) chains, a1, a2, a5 and a6, were demonstrated in BM beneath themesothelial cells of all types of SMs, whereas only capillary BM consisted of a1 and a2. Besides,epicardial SM expressed a3 and a4 moderately as extra components. The a(IV) chain composition was same as those of epidermal skin BM. Therefore, these a(IV)chains are designated to be essential for BM covering inside and outside of the body