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  • 81.20.-n  (1)
  • Ca2+ channel  (1)
  • Cytochrome P-450  (1)
  • 1
    ISSN: 0009-8981
    Schlagwort(e): Bile acid synthesis ; Cerebrotendinous xanthomatosis ; Cytochrome P-450 ; Ferredoxin ; Mitochondrial monooxygenase ; NADPH-ferredoxin reductase
    Quelle: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Thema: Medizin
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    ISSN: 1432-0630
    Schlagwort(e): 78.55.Cr ; 78.30.Gt ; 81.20.-n
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Maschinenbau , Physik
    Notizen: Abstract Mg+ ions were implanted into highly pure InP grown by the liquid encapsulated Czochralski (LEC) method in which the Mg concentration [Mg] was varied between 1×1015 cm−3 and 3×1020 cm–3. Two annealing methods were used: furnace annealing (FA) up to 740° C and flash lamp annealing (rapid thermal annealing, RTA) up to 900° C. For characterization, photoluminescence (PL) spectra were measured between 2K and room temperature together with Raman scattering measurements at room temperature. An emission designated by g, which was attributed to a novel energy state of an isolated acceptor, was found to be produced for a rather low value of [Mg]. In addition, a broad emission denoted by [g−g], which was ascribed to acceptor-acceptor pairs, was observed below bound exciton emissions for moderate values of [Mg]. These features were quite similar to those previously observed in acceptor-doped GaAs when the background concentration of donors is extremely low. Two additional novel emissions located far below the band-to-acceptor emission were also obtained, and each showed a remarkable energy shift towards lower energy with increasing [Mg]. The binding energies of these emissions were estimated from the temperature dependence of PL spectra and the results suggest that they are complex-type radiative recombination centers, presumably donor-acceptor-type centers. A strong broad emission centered near the band-to-acceptor emission was observed for [Mg]=3×1020 cm−3. This observation indicates a formation of a new material between In, P and Mg, which was also attested by the appearance of a new TO-like Raman signal for [Mg] greater than 1×1019 cm−3. A substantial difference of PL and Raman spectra was revealed for the two annealing methods, suggesting that the annealing behaviour of ion-implanted InP should be investigated more extensively in order to establish reliable annealing procedures.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    ISSN: 1432-2013
    Schlagwort(e): Key words Ruthenium red ; Smooth muscle ; Ca2+-dependent K+ channel ; Ca2+ channel ; Ryanodine ; Urinary bladder
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin
    Notizen: Abstract  Three major ionic currents, Ca2+-dependent K+ current (I K-Ca), delayed rectifier type K+ current (I kd) and Ca2+ current (I Ca), were activated by depolarization under whole-cell clamp in single smooth muscle cells isolated from guinea-pig urinary bladder. Externally applied ruthenium red (RuR) reduced the amplitude of I K-Ca and I Ca at 0 mV (IC50 values were 4.2 and 5.6 μM, respectively), but did not affect I Kd. Spontaneous transient outward currents (STOCs) and caffeine-induced outward currents (I caf) at –30 mV were reduced by external 10 μM RuR. When 10 μM RuR was added to the pipette solution, I K-Ca during depolarization, STOCs and I caf significantly decreased with time. RuR did not change the unitary current amplitude of the large-conductance Ca2+-dependent K+ (BK) channels, but reduced the open probability of the channel under excised patch-clamp recording mode. RuR reduced the channel activity more effectively from the cytosolic face than from the other. This inhibition decreased when the cytosolic Ca2+ concentration was increased. These results indicate that RuR blocks BK and Ca2+ channels in urinary bladder smooth muscle cells. The decrease in I K-Ca, STOCs and I caf by RuR is attributable to the direct inhibition of BK channel activity, probably in addition to the inhibition of Ca2+ release from storage sites. The direct inhibition of BK channel activity by RuR may be related to the interaction of RuR with the Ca2+-binding sites of the channel protein.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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