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  • 1990-1994  (3)
  • 1994  (3)
Material
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  • 1990-1994  (3)
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  • 1
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 65 (1994), S. 2060-2062 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We present high resolution measurements of the far infrared reflectance and absorbance of InAs/AlSb type II heterostructures, grown on GaAs substrates by molecular beam epitaxy. Quantum wells grown with AlAs-like interfaces show broadening and blue shifting of the InAs transverse optical (TO) phonon compared to samples with InSb-like interfaces. This is explained by incorporation of arsenic in the AlSb barriers. The InSb-interface mode, recently reported from Raman investigations, could be observed in the multiple quantum well. Two lines are observed, which are attributed to the normal (AlSb on InAs) and the inverted (InAs on AlSb) interfaces. © 1994 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 64 (1994), S. 1665-1667 
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: A photoluminescence study of InAs/AlSb single quantum well structures with a width varying between 20 and 5 nm is presented. Using Fourier-transform spectroscopy, the spatially indirect radiative recombination is observed. Excitation of the photoluminescence at 1.32 μm instead of excitation in the visible leads to broadening and blueshifting of the spectra. This behavior is explained by a photoinduced increase of the electron concentration. The optically induced blueshift of the low energy onset of the spectra is attributed to screening of an acceptor level in the AlSb barrier near the InAs/AlSb interface, located about 80 meV above the AlSb valence band maximum. The blueshift of the high energy of the luminescence spectra is limited to a transition energy of 420 meV, providing evidence for the existence of a deep level in the AlSb barriers.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of muscle research and cell motility 15 (1994), S. 29-36 
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Phalloidin was shown to increase the ATPase activity and Ca2+ sensitivity of both bovine cardiac and rabbit psoas myofibrils when assayed in a solution containing 50 mm KCl, 100 mm MOPS (pH 7.0), 2 mm MgCl2, 1 mm ATP, 2 mm EGTA, and varying concentrations of Ca2+ (temperature 21–22°C). The phalloidin effect in cardiac myofibrils developed over a time course of several minutes in the presence of 50 μm phalloidin. Relative increase of ATPase activity was maximal at pCa 8 and decreased with decrease in pCa. In cardiac myofibrils the increase was about 70% at pCa 8 and 20% at pCa 4 following 20–30 min pre-incubation with 2 μm or 50 μm phalloidin. The effect persisted after excess phalloidin was washed out. The increase in Ca2+ sensitivity was approximately 0.15 pCa units. For skeletal myofibrils treated with 2 μm phalloidin all changes were considerably less than those seen with cardiac myofibrils and the changes were even less when the myofibrils were exposed to 50 μm phalloidin. These results show that when specifically bound to actin, phalloidin can change the kinetic parameters of the cross-bridge cycle and may also alter the Ca2+ sensitivity of the contractile system. The effects of phalloidin seem to vary with muscle type.
    Type of Medium: Electronic Resource
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