254 research outputs found

    Investigation of Horizontal Velocity Fields in Stirred Vessels with Helical Coils by PIV

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    Horizontal velocity flow fields were measured by particle image velocimetry for a stirred vessel with baffles and two helical coils for enlargement of heat transfer area. The investigation was carried out in a cylindrical vessel with flat base and two different stirrers (radial-flow Rushton turbine and axial-flow propeller stirrer). Combined velocity plots for flow fields at different locations are presented. It was found that helical coils change the flow pattern significantly. Measurements for the axial-flow Rushton turbine showed a strong deflection by the coils, leading to a mainly tangential flow pattern. Behind baffles large areas of unused heat transfer area were found. First results for the axial-flow propeller reveal an extensive absence of fluid movement in the horizontal plane. Improved design considerations for enhanced heat transfer by more compatible equipment compilation are proposed

    Magnetic domain structure of epitaxial Ni-Mn-Ga films

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    For the magnetic shape memory effect, knowledge about the interaction between martensitic and magnetic domain structure is essential. In the case of Ni-Mn-Ga bulk material and foils, a staircase-like magnetic domain structure with 90{\deg}- and 180{\deg}-domain walls is known for modulated martensite. In the present paper we show that the magnetic domain pattern of thin epitaxial films is fundamentally different. Here we analyze epitaxial Ni-Mn-Ga films by atomic and magnetic force microscopy to investigate the correlation between the twinned martensitic variants and the magnetic stripe domains. The observed band-like domains with partially perpendicular outof-plane magnetization run perpendicular to the microstructure domains defined by twinning variants. These features can be explained by the finite film thickness, resulting in an equilibrium twinning period much smaller than the domain period. This does not allow the formation of a staircase domain patter. Instead the energies of the magnetic and martensitic microstructures are minimized independently by aligning both patterns perpendicularly to each other. By analyzing a thickness series we can show that the observed magnetic domain pattern can be quantitatively described by an adapted band domain model of Kittel.Comment: 12 pages, 4 figure

    Structural genomics of human proteins – target selection and generation of a public catalogue of expression clones

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    BACKGROUND: The availability of suitable recombinant protein is still a major bottleneck in protein structure analysis. The Protein Structure Factory, part of the international structural genomics initiative, targets human proteins for structure determination. It has implemented high throughput procedures for all steps from cloning to structure calculation. This article describes the selection of human target proteins for structure analysis, our high throughput cloning strategy, and the expression of human proteins in Escherichia coli host cells. RESULTS AND CONCLUSION: Protein expression and sequence data of 1414 E. coli expression clones representing 537 different proteins are presented. 139 human proteins (18%) could be expressed and purified in soluble form and with the expected size. All E. coli expression clones are publicly available to facilitate further functional characterisation of this set of human proteins

    Development of Dietary-Based Toxicity Reference Values to Assess the Risk of Chlorophacinone to Non-Target Raptorial Birds

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    Regulatory changes in the use of some second-generation anticoagulant rodenticides in parts of North America may result in expanded use of first-generation anticoagulant rodenticides (FGARs). Recent toxicological studies with captive raptors have demonstrated that these species are considerably more sensitive to the FGAR diphacinone than traditional avian wildlife test species (mallard, bobwhite). We have now examined the toxicity of the FGAR chlorophacinone (CPN) to American kestrels fed rat tissue mechanically amended with CPN, or rat tissue containing biologically-incorporated CPN, for 7 days. Nominal CPN concentrations in these diets were 0.15, 0.75, and 1.5 μg/g food wet weight, and actual CPN concentration in diets were analytically verified as being close to target values. Food intake was consistent among groups, body weight fluctuated by less than 6%, exposure and adverse effects were generally dose-dependent, and there were no dramatic differences in toxicity between mechanically-amended and biologically-incorporated CPN diets. Using benchmark dose statistical methods, toxicity reference values at which clotting times were prolonged in 50% of the kestrels was estimated to be about 80 μg CPN consumed/kg body weight-day for prothrombin time and 40 μg CPN/kg body weight-day for Russell’s viper venom time. Based upon carcass CPN residues reported in rodents from field baiting studies, empirical measures of food consumption in kestrels, and dietary-based toxicity reference values derived from the 7-day exposure scenario, some free-ranging raptors consuming CPN-exposed prey might exhibit coagulopathy and hemorrhage. These sublethal responses associated with exposure to environmentally realistic concentrations of CPN could compromise survival of exposed birds

    Toxicity reference values for chlorophacinone and their application for assessing anticoagulant rodenticide risk to raptors

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    Despite widespread use and benefit, there are growing concerns regarding hazards of second-generation anticoagulant rodenticides to non-target wildlife which may result in expanded use of first-generation compounds, including chlorophacinone (CPN). The toxicity of CPN over a 7-day exposure period was investigated in American kestrels (Falco sparverius) fed either rat tissue mechanically- amended with CPN, tissue from rats fed Rozol bait (biologically-incorporated CPN), or control diets (tissue from untreated rats or commercial bird of prey diet) ad libitum. Nominal CPN concentrations in the formulated diets were 0.15, 0.75 and 1.5 µg/g food wet weight, and measured concentrations averaged 94 % of target values. Kestrel food consumption was similar among groups and body weight varied by less than 6 %. Overt signs of intoxication, liver CPN residues, and changes in prothrombin time (PT), Russell’s viper venom time (RVVT) and hematocrit, were generally dose-dependent. Histological evidence of hemorrhage was present at all CPN dose levels, and most frequently observed in pectoral muscle and heart. There were no apparent differences in toxicity between mechanically-amended and biologically-incorporated CPN diet formulations. Dietary-based toxicity reference values at which clotting times were prolonged in 50 % of the kestrels were 79.2 µg CPN consumed/kg body weight-day for PT and 39.1 µg/kg body weight-day for RVVT. Based upon daily food consumption of kestrels and previously reported CPN concentrations found in small mammals following field baiting trials, these toxicity reference values might be exceeded by free-ranging raptors consuming such exposed prey. Tissue-based toxicity reference values for coagulopathy in 50 % of exposed birds were 0.107 µg CPN/g liver wet weight for PT and 0.076 µg/g liver for RVVT, and are below the range of residue levels reported in raptor mortality incidents attributed to CPN exposure. Sublethal responses associated with exposure to environmentally realistic concentrations of CPN could compromise survival of free-ranging raptors, and should be considered in weighing the costs and benefits of anticoagulant rodenticide use in pest control and eradication programs
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