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        Physical Model Investigation of a Compact Waste Water Pumping Station

        Kirst, Kilian,Hellmann, D.H.,Kothe, Bernd,Springer, Peer Korean Society for Fluid machinery 2010 International journal of fluid machinery and syste Vol.3 No.4

        To provide required flow rates of cooling or circulating water properly, approach flow conditions of vertical pump systems should be in compliance with state of the art acceptance criteria. The direct inflow should be vortex free, with low pre-rotation and symmetric velocity distribution. Physical model investigations are common practice and the best tool of prediction to evaluate, to optimize and to document flow conditions inside intake structures for vertical pumping systems. Optimization steps should be accomplished with respect to installation costs and complexity on site. The report shows evaluation of various approach flow conditions inside a compact waste water pumping station. The focus is on the occurrence of free surface vortices and the evaluation of air entrainment for various water level and flow rates. The presentation of the results includes the description of the investigated intake structure, occurring flow problems and final recommendations.

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        Cold but not too cold: advances in hypothermic and normothermic organ perfusion

        Guenter Kirste 대한이식학회 2022 Korean Journal of Transplantation Vol.36 No.1

        Transplantation is the method of choice and, in many cases, the only method of treatment for patients with end-stage organ disease. Excellent results have been achieved, and the main focus today is to extend the number of available donors. The use of extended- criteria donors or donors after circulatory death is standard, but is accompanied by an increased risk of ischemia reperfusion injury. This review presents newly developed machine perfusion techniques using hypothermic, subnormothermic, or normothermic conditions, with or without oxygenation. Possibilities for treatment and quality assessment in decision-making about organ acceptability are also discussed.

      • Deletion of the chloroplast LTD protein impedes LHCI import and PSI–LHCI assembly in <i>Chlamydomonas reinhardtii</i>

        Jeong, Jooyeon,Baek, Kwangryul,Yu, Jihyeon,Kirst, Henning,Betterle, Nico,Shin, Woongghi,Bae, Sangsu,Melis, Anastasios,Jin, EonSeon Oxford University Press 2018 Journal of experimental botany Vol.69 No.5

        <▼1><P>The <I>Chlamydomonas reinhardtii</I> LTD null mutant generated by CRISPR–Cas9, displayed aberrant PSI–LHCI holocomplexes, suggesting that the LTD protein may selectively function in PSI–LHCI assembly in green microalgae</P></▼1><▼2><P><B>Abstract</B></P><P>Nuclear-encoded light-harvesting chlorophyll- and carotenoid-binding proteins (LHCPs) are imported into the chloroplast and transported across the stroma to thylakoid membrane assembly sites by the chloroplast signal recognition particle (CpSRP) pathway. The LHCP translocation defect (LTD) protein is essential for the delivery of imported LHCPs to the CpSRP pathway in <I>Arabidopsis</I>. However, the function of the LTD protein in <I>Chlamydomonas reinhardtii</I> has not been investigated. Here, we generated a <I>C. reinhardtii ltd</I> (<I>Crltd</I>) knockout mutant by using CRISPR–Cas9, a new target-specific knockout technology. The <I>Crltd1</I> mutant showed a low chlorophyll content per cell with an unusual increase in appressed thylakoid membranes and enlarged cytosolic vacuoles. Profiling of thylakoid membrane proteins in the <I>Crltd1</I> mutant showed a more severe reduction in the levels of photosystem I (PSI) core proteins and absence of functional LHCI compared with those of photosystem II, resulting in a much smaller PSI pool size and diminished chlorophyll antenna size. The lack of CrLTD did not prevent photoautotrophic growth of the cells. These results are substantially different from those for Arabidopsis <I>ltd</I> null mutant, indicating LTD function in LHCP delivery and PSI assembly may not be as stringent in <I>C. reinhardtii</I> as it is in higher plants.</P></▼2>

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