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  • American Institute of Physics (AIP)  (1)
  • Springer  (1)
  • Springer Nature
  • 1990-1994  (2)
  • 1
    Digitale Medien
    Digitale Medien
    [S.l.] : American Institute of Physics (AIP)
    Review of Scientific Instruments 63 (1992), S. 1973-1977 
    ISSN: 1089-7623
    Quelle: AIP Digital Archive
    Thema: Physik , Elektrotechnik, Elektronik, Nachrichtentechnik
    Notizen: A space qualified 260° spherical plate electrostatic analyzer has been developed as a plasma diagnostic tool. The use of nested spheres and unusually shaped microchannel plates has resulted in a sensor capable of measuring simultaneously the three-dimensional populations of ions and electrons in a plasma. High-current microchannel plates and a new packaging of a hybrid preamplifier discriminator are combined with an uncommon high-voltage circuit. The combination of these features yields an analyzer that is compact and lightweight, efficient in its power consumption, and has a broad dynamic range.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Planta 186 (1991), S. 44-51 
    ISSN: 1432-2048
    Schlagwort(e): Embryo (peptide carrier) ; Hordeum (embryo, peptide transport) ; Peptide transport ; Photoaffinity probe
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract The preparation of a phenylalanine analogue containing an azido group and its incorporation into dipeptides is described. Peptides modified in this way are taken up into barley (Hordeum vulgare L.) scutella via the previously characterized peptide-transport system. Photoactivation of modified peptides in the presence of isolated scutella resulted in irreversible inhibition of peptide uptake in a concentration-dependent manner. Transport of other solutes which share a common mechanism of energy coupling, but which are transported via distinct carriers, was not inhibited after photo-derivatization of scutella with the modified peptides. Derivatization of isolated scutellar tissue with a 14C-labelled peptide analogue, resulted in incorporation of label into two proteins of Mr = 54000 and 41000. Scutellar tissue from early-germinating seeds, which do not show active peptide uptake, did not incorporate label into these polypeptides. It is concluded that these proteins are components of the barley peptide-transport system.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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