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  • 1
    Electronic Resource
    Electronic Resource
    Study of photoreaction processes of PDA Langmuir films (1988)
    s.l. : American Chemical Society
    Langmuir 4 (1988), S. 903-906 
    Details
    ISSN: 1520-5827
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/la00082a021
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  • 2
    Electronic Resource
    Electronic Resource
    Polymerization and submicron pattern fabrication on saturated and unsaturated fatty acid LB films using x-ray irradiation (1988)
    s.l. : American Chemical Society
    Langmuir 4 (1988), S. 1229-1233 
    Details
    ISSN: 1520-5827
    Source: ACS Legacy Archives
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/la00084a002
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Time-of-flight measurement of excitonic polaritons in a GaAs/AlGaAs quantum well (1988)
    Woodbury, NY : American Institute of Physics (AIP)
    Applied Physics Letters 53 (1988), S. 1077-1079 
    Details
    ISSN: 1077-3118
    Source: AIP Digital Archive
    Topics: Physics
    Notes: We report the first experimental observation of excitonic polaritons in a GaAs/AlGaAs quantum well with incident light propagating parallel to the quantum well layer. We have built a time-of-flight measurement system which allows us to investigate low-temperature optical properties of semiconductor waveguides with picosecond time resolution. This system has been used to measure propagation delay time of an incident light pulse transmitted through the quantum well. The delay time increases drastically near the photon energies resonant to the optical absorption lines of the quantum well excitons. This behavior shows that the group velocity of the light pulse decreases as a result of the formation of quantum well excitonic polaritons. The group velocity drops to 7×104 m/s at a heavy-hole exciton absorption line at 6.0 K.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.100071
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Low- and high-temperature structure of (E)-2,2'-dimethylstilbene (1988)
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 44 (1988), S. 505-508 
    Details
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1107/S0108270187011132
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Smooth muscle cells of the chicken aortic arch differ from those in the gizzard and the femoral artery in the distribution of F-actin, α-actinin and filamin (1988)
    Springer
    Histochemistry and cell biology 88 (1988), S. 525-532 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of F-actin, α-actinin and filamin in smooth muscle cells of the chicken was examined by immunofluorescent and immunoelectron microscopy. Those from the gizzard, the femoral artery and the aortic arch were compared. F-Actin labeled by NBD-phallacidin was seen diffusely distributed in the sarcoplasm in the gizzard and the femoral artery, but in the aorta it was observed as streaks and spots, with unstained areas in between. Epon sections of the aortic arch showed that bundles of thin myofilaments run in various directions interspersed with areas mostly occupied by intermediate filaments. α-Actinin labelling occurred in dense plaques along the sarcolemma in all the muscles examined. While dense bodies in the sarcoplasm were common and labelled for α-actinin in the gizzard and the femoral artery, hardly any were seen in the aortic arch and little labelling for α-actinin was observed in the sarcoplasm. Filamin was concentrated along the periphery of dense bodies and plaques in the gizzard and the femoral artery, but it was seen diffusely in the sarcoplasm of the aortic muscle. After chemical skinning of the latter, filamin labelling persisted only in the F-actin bundles, and other areas became negative. The present results show that smooth muscle cells of the aortic arch contrast with those of the gizzard and even with those of the femoral artery in the distribution of F-actin, α-actinin and filamin. The mechanisms of contraction and/or stress maintenance in the aortic smooth muscle may be different from those in other smooth muscles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00570320
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  • 6
    Electronic Resource
    Electronic Resource
    Radiation effect of a high energy electron beam on thin films of saturated and unsaturated fatty acids (1988)
    Springer
    Colloid & polymer science 266 (1988), S. 525-531 
    Details
    ISSN: 1435-1536
    Keywords: Arachidic acid (ADA) ; ω-tricosenoic acid (TSA) ; ω-tricocynoic acid (TCA) ; electron beam irradiation ; FTIR spectrophotometry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: Abstract Studies have been carried out on electron beam induced polymerization of LB films of saturated and unsaturated long chain aliphatic acids, in an attempt to obtain information about the dose dependence of conversion in relation to molecular arrangement. The results indicate that polymerization of unsaturated aliphatic acid LB films occurred when irradiation was carried out in a nitrogen atmosphere and that the LB films of a disordered state are more sensitive to radiation than tightly packed LB films.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01420763
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  • 7
    Electronic Resource
    Electronic Resource
    Effects of phospholipase inhibitors and calcium antagonists on the changes in myocardial phospholipids induced by isoproterenol (1988)
    Springer
    Basic research in cardiology 83 (1988), S. 567-575 
    Details
    ISSN: 1435-1803
    Keywords: isoproterenol ; myocardialphospholipid ; phospholipase inhibitor ; calcium antagonist ; β-blocker
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary To investigate the change in myocardial phospholipids after the administration of isoproterenol and its prevention by pretreatment with phospholipase inhibitors and calcium antagonists, we determined the phospholipid species in the heart of female Wistar rats. Isoproterenol (40 mg/kg) was administered 24 h before excising the heart, and chlorpromazine, mepacrine (phospholipase inhibitors), nifedipine, verapamil (calcium antagonists) and propranolol (β-adrenoceptor blocker) were injected intraperitoneally 30 min prior to isoproterenol administration. The phospholipid species were quantified using silica gel precoated thin-layer rods and the hydrogen flame ionization method. Isoproterenol induced significant increases in heart/body weight ratio, myocardial protein/heart weight ratio and lysophosphatidylcholine (LPC), and significant decreases in myocardial total phosphorus, creatine kinase (CK) activity, phosphatidylethanolamine and phosphatidylcholine (PC). The significant decrease in PC and increase in LPC indicated the degradation of myocardial phospholipids. Pretreatment with nifedipine (30 mg/kg), verapamil (50 mg/kg) or propranolol (20 mg/kg) completely prevented the occurrence of myocardial injury through the preservation of myocardial phospholipid composition, total phosphorus, CK activity and heart/body and protein/heart weight ratios. On the other hand, chlorpromazine (30 mg/kg) and mepacrine (50 mg/kg) partially prevented myocardial damage through the preservation of myocardial phospholipid composition, total phosphorus and CK activity. Results suggest that not only calcium influx but also phospholipase activation plays an important role in the development of myocardial injury induced by isoproterenol.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01906686
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