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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Journal of fusion energy 19 (2000), S. 143-157 
    ISSN: 1572-9591
    Keywords: Plasma focus ; tailored X-ray source
    Source: Springer Online Journal Archives 1860-2000
    Topics: Energy, Environment Protection, Nuclear Power Engineering
    Notes: Abstract A low-energy (2.3 kJ) plasma focus energized by a single 32-μF capacitor charged at 12 kV with filling gases hydrogen, neon, and argon is investigated as an X-ray source. Experiments are conducted with a copper and an aluminum anode. Specifically, attention is given to tailoring the radiation in different windows, e.g., 1.2–1.3 keV, 1.3–1.5 keV, 2.5–5 keV, and Cu-Kα line radiation. The highest X-ray emission is observed with neon filling and the copper anode in the 1.2–1.3 keV window, which we speculate to be generated due to recombination of hydrogenlike neon ions with a few eV to a few 10s of eV electrons. The wall-plug efficiency of the device is found to be 4%. The other significant emission occurs with hydrogen filling, which exhibits wall-plug efficiency of 1.7% for overall X-ray emission and 0.35% for Cu-Kα line radiation. The emission is dominated by the interaction of electrons in the current sheath with the anode tip. The emission with the aluminum anode and hydrogen filling is up to 10 J, which corresponds to wall-plug efficiency of 0.4%. The X-ray emission with argon filling is less significant.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular and cellular biochemistry 87 (1989), S. 171-183 
    ISSN: 1573-4919
    Keywords: acid phosphatase ; subcellular fractionation ; Percoll gradient ; GERL ; Prelysosomes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary Lysosomes are defined traditionally with the marker enzyme acid phosphatase. We showed recently that lysosomes from human fibroblasts can be separated into a light and dense fraction as well as prelysosomal population. We now provide evidence that although acid phosphatase is enriched in all three fractions, the marker enzyme in the prelysosomal compartment is qualitatively distinct from that of the lysosomes. Ultrastructural analysis showed that the acid phosphatase in the prelysosomal vesicles deposited an extremely electron-dense reaction product, entirely obliterating the lumen of the vesicle, in contrast to that of the light and dense lysosomes which deposited a fine and diffuse product scattered throughout the luminal space. Biochemical analysis showed that only 51% of the acid phosphatase in the prelysosomes was inhibited by tartrate, while 80% of that in the lysosomes was tartrate-inhibitable. Immunoprecipitation with antibodies specific for various isozymes of acid phosphatase showed that 39% of the acid phosphatase in the prelysosomes was of the ‘lysosomal’ type whereas over 5007o of the acid phosphatase in the lysosomes was of this type. These results showed that acid phosphatase in the prelysosomes of human cultured fibroblasts can be distinguished from that of the lysosomes cytochemically, biochemically, and immunologically and that lysosomes, as marked by acid phosphatase, are a heterogeneous organelle.
    Type of Medium: Electronic Resource
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