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  • 52.75Kq  (1)
  • Na,K-ATPase  (1)
  • Springer  (2)
  • Wiley-Blackwell
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied physics 16 (1978), S. 425-432 
    ISSN: 1432-0630
    Keywords: 52.75Kq ; 52.25Dg ; 52.80Mg
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Particle densities are determined for a decaying axially blown SF6 are between current zero and brekdown, some 100 μs later. During the time of interest, primarily only atoms, diatomic molecules and ions can be built up by reactions. Therefore, in a first approach equilibrium densities are derived for SF6 which has decomposed into its considemic and diatomic components. In a second approach reaction kinetics are considered. It turns out that the development of densities occurs in two steps. During the first approx. 100 μs there is a strong deviation from equilibrium. Afterwards the most abundant particles remain near their partial, diatomic equilibrium values. Near breakdown the degree of ionization is of the order of 1013 cm−3 with the most abundant ions S 2 + and F−. This density is sufficient to distort the applied electric field. Future theories of breakdown in hot gases must take into account this principal difference as compared with the conditions in cold gases.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4994
    Keywords: Na,K-ATPase ; fluorescent inhibitor ; kinetics ; energy transfer
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract The interaction between the fluorescent ouabain derivative DEDO and purified renal Na,K-ATPase (isolated from different animal species) is investigated. Equilibrium binding studies provide a pK value of about 7.5 and a stoichoimetric coefficient of 1. Nonmodified ouabain exhibits the same affinity to the rabbit enzyme; the enzyme originating from the other sources binds DEDO 10 times less strongly than ouabain. Kinetic studies indicate that this is the consequence of a 10 times higher dissociation rate constant of the complexes formed with DEDO. The fluorescence emission intensity of DEDO is enhanced, being dependent on the enzyme source. The single decay time of DEDO is 3 ns in the absence and 21 ns in the presence of the rabbit enzyme and 14 ns in the presence of the pig renal enzyme. This result suggests that the fluorophore of DEDO is bound to a very hydrophobic environment of the enzyme. Further characterization of the static fluorescence spectra provides evidence for energy transfer between Trp residues of the enzyme and DEDO. Distance estimations suggest that one or two Trp residues are likely to be located in the proximity of the fluorophore.
    Type of Medium: Electronic Resource
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