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Träfflista för sökning "WFRF:(Engel Andreas) srt2:(2001-2004)"

Sökning: WFRF:(Engel Andreas) > (2001-2004)

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2.
  • Johnsson, Filip, 1960, et al. (författare)
  • In-furnace processes in a 235 MWe CFB boiler
  • 2002
  • Ingår i: Proc. of the 7th International Conference on Circulating Fluidized Beds. - 9780920804988 ; , s. 607-614
  • Konferensbidrag (refereegranskat)abstract
    • In an experimental project funded by the 5th Framework Programme of the European Community (EC), different measurement techniques are used to analyze in-furnace processes in a 235 MWe Circulating Fluidized Bed (CFB) boiler in Turow, Poland. The purpose of the project is to assess the insufficiently known features of large-scale CFB boilers. The furnace of the boiler has a cross-section of 21 x 10 meters and a height of 43 meters. The boiler is operated on a local brown coal. Steady state, as well as dynamic conditions, are studied. The project is unique in two respects: Firstly, several measurement ports are provided in the large CFB furnace for in-situ measurements in various locations on the furnace. Secondly, a number of measurement techniques are employed. These facilitate studies of hydrodynamic processes as well as local variations in gas components (such as O2, CO, THC) and solids materials. The paper describes the measurement techniques and provides examples of the first (hydrodynamic) results obtained by the in-situ measurements.
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3.
  • Karlsson, Maria, 1985, et al. (författare)
  • Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris.
  • 2003
  • Ingår i: FEBS Letters. - 1873-3468 .- 0014-5793. ; 537:1-3, s. 68-72
  • Tidskriftsartikel (refereegranskat)abstract
    • The aquaporin PM28A is one of the major integral proteins in spinach leaf plasma membranes. Phosphorylation/dephosphorylation of Ser274 at the C-terminus and of Ser115 in the first cytoplasmic loop has been shown to regulate the water channel activity of PM28A when expressed in Xenopus oocytes. To understand the mechanisms of the phosphorylation-mediated gating of the channel the structure of PM28A is required. In a first step we have used the methylotrophic yeast Pichia pastoris for expression of the pm28a gene. The expressed protein has a molecular mass of 32462 Da as determined by matrix-assisted laser desorption ionization-mass spectrometry, forms tetramers as revealed by electron microscopy and is functionally active when reconstituted in proteoliposomes. PM28A was efficiently solubilized from urea- and alkali-stripped Pichia membranes by octyl-beta-D-thioglucopyranoside resulting in a final yield of 25 mg of purified protein per liter of cell culture.
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