Unsteady Diffusion Flames: Ignition, Travel, and Burnout (SUBCORE Project: Simplified Unsteady Burning of Contained Reactants)

An experimental apparatus for the examination of a planar, virtually strain-rate-free diffusion flame in microgravity has been designed and fabricated. Such a diffusion flame is characterized by relatively large spatial scale and high symmetry (to facilitate probing), and by relatively long fluid-residence time (to facilitate investigation of rates associated with sooting phenomena). Within the squat rectangular apparatus, with impervious, noncatalytic isothermal walls of stainless steel, a thin metallic splitter plate subdivides the contents into half-volumes. One half-volume initially contains fuel vapor diluted with an inert gas, and the other, oxidizer diluted with another inert gas-so that the two domains have equal pressure, density, and temperature. As the separator is removed, by translation in its own plane, through a tightly fitting slit in one side wall, a line ignitor in the opposite side wall initiates a triple-flame propagation across the narrow layer of combustible mixture formed near midheight in the chamber. The planar diffusion flame so emplaced is quickly disrupted in earth gravity. In microgravity, the planar flame persists, and travels ultimately into the half-volume containing the stoichiometrically deficient reactant; the flame eventually becomes extinguished owing to reactant depletion and heat loss to the walls

Transendothelial glucose transport is not restricted by extracellular hyperglycaemia

Endothelial cells are routinely exposed to elevated glucose concentrations post-prandially in healthy individuals and permanently in patients with metabolic syndrome and diabetes, and so we assessed their sugar transport capabilities in response to high glucose. In human umbilical vein (HUVEC), saphenous vein, microdermal vessels and aorta, GLUT1 (SLC2A1), GLUT3 (SLC2A3), GLUT6 (SLC2A6), and in microdermal vessels also GLUT12 (SLC2A12), were the main glucose transporters as assessed by mRNA, with no fructose transporters nor SGLT1 (SLC5A1). Uptake of 14C-fructose was negligible. GLUT1 and GLUT3 proteins were detected in all cell types and were responsible for ~ 60% glucose uptake in HUVEC, where both GLUT1 and GLUT3, but not GLUT6 siRNA knock-down, reduced the transport. Under shear conditions, GLUT1 protein decreased, GLUT3 increased, and 14C-deoxy-glucose uptake was attenuated. In high glucose, lipid storage was increased, cell numbers were lower, 14C-deoxy-glucose uptake decreased owing to attenuated GLUT3 protein and less surface GLUT1, and trans-endothelial transport of glucose increased due to cell layer permeability changes. We conclude that glucose transport by endothelial cells is relatively resistant to effects of elevated glucose. Cells would continue to supply it to the underlying tissues at a rate proportional to the blood glucose concentration, independent of insulin or fructose

Die geographische Verbreitung der Schutzhütten und Unterkunftshäuser in den Ostalpen

vorgelegt von Rungaldier RudolfText handschriftl.Graz, Univ., Diss., 1920(VLID)470134

Bewässerungssysteme im Alpenraum - zwischen Tradition und Moderne

eingereicht von Mag.a Eva Maria Rungaldier, BScLiteraturverzeichnis: Blatt 97-104Zusammenfassung/Abstract in deutscher und englischer SpracheParis-Lodron-Universität Salzburg, Masterarbeit, 2018(VLID)500313

Binding of [³H]photocholesterol to wildtype and mutant stomatin.

<p>COS-7 cells were transiently transfected with WT or mutant stomatin constructs. Subsequently they were incubated with a photoactivatable, radioactive cholesterol derivative ([³H]photocholesterol) and irradiated with UV light to crosslink [³H]photocholesterol to respective binding proteins. The cells were solubilized and stomatin was immunoprecipitated by monoclonal anti-stomatin antibody GARP-50. (<b>A</b>) SDS-PAGE and autoradiography revealed cholesterol-binding to WT and mutant stomatin. (<b>B</b>) The expression level of the constructs was determined by immunoblotting with monoclonal anti-stomatin antibody GARP-50.</p

Structure-function analysis of human stomatin: A mutation study

<div><p>Stomatin is an ancient, widely expressed, oligomeric, monotopic membrane protein that is associated with cholesterol-rich membranes/lipid rafts. It is part of the SPFH superfamily including stomatin-like proteins, prohibitins, flotillin/reggie proteins, bacterial HflK/C proteins and erlins. Biochemical features such as palmitoylation, oligomerization, and hydrophobic “hairpin” structure show similarity to caveolins and other integral scaffolding proteins. Recent structure analyses of the conserved PHB/SPFH domain revealed amino acid residues and subdomains that appear essential for the structure and function of stomatin. To test the significance of these residues and domains, we exchanged or deleted them, expressed respective GFP-tagged mutants, and studied their subcellular localization, molecular dynamics and biochemical properties. We show that stomatin is a cholesterol binding protein and that at least two domains are important for the association with cholesterol-rich membranes. The conserved, prominent coiled-coil domain is necessary for oligomerization, while association with cholesterol-rich membranes is also involved in oligomer formation. FRAP analyses indicate that the C-terminus is the dominant entity for lateral mobility and binding site for the cortical actin cytoskeleton.</p></div

Binding of [³H]photocholesterol to wildtype and mutant stomatin.

<p>COS-7 cells were transiently transfected with WT or mutant stomatin constructs. Subsequently they were incubated with a photoactivatable, radioactive cholesterol derivative ([³H]photocholesterol) and irradiated with UV light to crosslink [³H]photocholesterol to respective binding proteins. The cells were solubilized and stomatin was immunoprecipitated by monoclonal anti-stomatin antibody GARP-50. (<b>A</b>) SDS-PAGE and autoradiography revealed cholesterol-binding to WT and mutant stomatin. (<b>B</b>) The expression level of the constructs was determined by immunoblotting with monoclonal anti-stomatin antibody GARP-50.</p

Comparison of stomatin structural changes and functional consequences referring to wildtype.

<p>Comparison of stomatin structural changes and functional consequences referring to wildtype.</p