56 research outputs found

    Tests on Models of Nuclear Reactor Elements - Head Losses in Core Sub-Assemblies

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    Losses have been determined for flow through models of various proposed core sub-assemblies as part of a study of the elements of a nuclear reactor. Six core sections and two? axial blanket sub-assemblies have been compared on the basis of drop in piezometric. head or pressure drop. The core sub-assemblies are composed of an entrance nozzle, a lower axial blanket section, the core section, an upper axial blanket section, and a short section for the handling lug. The four parts of the sub-assembly other than the core section are designated as the axial blanket sub-assembly. In each core section there are 144 rods within a container which has a square cross-section. The primary differences between one core section and another are the means qf supporting and spacing the rods. Bars or wires wrapped in spirals around the rods were used as well as a series of grids made up of wires and supported at the four corners. Also, in one core an, inner wall was used to provide an annular flow passage which helps to reduce the difference in temperature at the inner and outer walls of the core. The two axial blanket sub-assemblies tested are similar except ?that the second model is characterized by more gradual transitions in changes of cross section. Other parts of this study of the elements of a nuclear reactor have been described in two previous reports dealing with head losses in complete blanket subassemblies and with diffusion studies

    Site-Specific Labeling of Annexin V with F-18 for Apoptosis Imaging

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    Annexin V is useful in detecting apoptotic cells by binding to phosphatidylserine (PS) that is exposed on the outer surface of the cell membrane during apoptosis. In this study, we examined the labeling of annexin V-128, a mutated form of annexin V that has a single cysteine residue at the NH2 terminus, with the thiol-selective reagent 18F-labeling agent N-[4-[(4-[18F]fluorobenzylidene)aminooxy]butyl]maleimide ([18F]FBABM). We also examined the cell binding affinity of the 18F-labeled annexin V-128 ([18F]FAN-128). [18F]FBABM was synthesized in two-step, one-pot method modified from literature procedure. (Toyokuni et al., Bioconjugate Chem. 2003, 14, 1253−1259). The average yield of [18F]FBABM was 23 ± 4% (n = 4, decay-corrected) and the specific activity was ∼6000 Ci/mmol. The total synthesis time was ∼92 min. The critical improvement of this study was identifying and then developing a purification method to remove an impurity N-[4-[(4-dimethylaminobenzylidene)aminooxy]butyl]maleimide 4, whose presence dramatically decreased the yield of protein labeling. Conjugation of [18F]FBABM with the thiol-containing annexin V-128 gave [18F]FAN-128 in 37 ± 9% yield (n = 4, decay corrected). Erythrocyte binding assay of [18F]FAN-128 showed that this modification of annexin V-128 did not compromise its membrane binding affinity. Thus, an in vivo investigation of [18F]FAN-128 as an apoptosis imaging agent is warranted

    Effects of Ethanol and NAP on Cerebellar Expression of the Neural Cell Adhesion Molecule L1

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    The neural cell adhesion molecule L1 is critical for brain development and plays a role in learning and memory in the adult. Ethanol inhibits L1-mediated cell adhesion and neurite outgrowth in cerebellar granule neurons (CGNs), and these actions might underlie the cerebellar dysmorphology of fetal alcohol spectrum disorders. The peptide NAP potently blocks ethanol inhibition of L1 adhesion and prevents ethanol teratogenesis. We used quantitative RT-PCR and Western blotting of extracts of cerebellar slices, CGNs, and astrocytes from postnatal day 7 (PD7) rats to investigate whether ethanol and NAP act in part by regulating the expression of L1. Treatment of cerebellar slices with 20 mM ethanol, 10−12 M NAP, or both for 4 hours, 24 hours, and 10 days did not significantly affect L1 mRNA and protein levels. Similar treatment for 4 or 24 hours did not regulate L1 expression in primary cultures of CGNs and astrocytes, the predominant cerebellar cell types. Because ethanol also damages the adult cerebellum, we studied the effects of chronic ethanol exposure in adult rats. One year of binge drinking did not alter L1 gene and protein expression in extracts from whole cerebellum. Thus, ethanol does not alter L1 expression in the developing or adult cerebellum; more likely, ethanol disrupts L1 function by modifying its conformation and signaling. Likewise, NAP antagonizes the actions of ethanol without altering L1 expression

    The use of computers in naval architecture education

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    http://deepblue.lib.umich.edu/bitstream/2027.42/8368/5/bad6042.0001.001.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/8368/4/bad6042.0001.001.tx

    Experimental investigation of green sea loadings on deckhouse geometry for a destroyer-type model

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    http://deepblue.lib.umich.edu/bitstream/2027.42/8367/5/bad6098.0001.001.pdfhttp://deepblue.lib.umich.edu/bitstream/2027.42/8367/4/bad6098.0001.001.tx
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