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  • Cell & Developmental Biology  (2)
  • 35  (1)
  • 2020-2023
  • 1985-1989  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Calorimetric absorption spectroscopy of J-aggregate dye monolayers below 0.1 Kelvin (1985)
    Springer
    Applied physics 38 (1985), S. 199-203 
    Details
    ISSN: 1432-0649
    Keywords: 42.80 ; 35 ; 07
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract We describe an extremely sensitive method to investigate nonradiative processes following optical excitation. In a low-temperature calorimeter, the sample is irradiated with monochromatic light. The absorbed energy which is converted into phonons leads to a measurable increase of the sample temperature. The lowest detectable dissipated energy is 2·10−12J at a working temperature of 0.03 K. We demonstrate our method with a calorimetric absorption spectrum of J-aggregate monolayers of 1-methyl-1′-octadecyl-2,2′-cyanine. From this spectrum the emission quantum efficiency is obtained as a function of excitation wavelength. A relative minimum is found at the long wavelength edge of the absorption band at 582.5 nm.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00697484
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  • 2
    Electronic Resource
    Electronic Resource
    Pharmacological profile of the substituted beta-lactam L-659,286: A member of a new class of human PMN elastase inhibitors (1989)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 39 (1989), S. 47-53 
    Details
    ISSN: 0730-2312
    Keywords: elastase inhibitors ; β-lactams ; lung damage ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human polymorphonuclear leukocyte elastase (PMN elastase) is inhibited by L-659, 286 (7α-methoxy-8-oxo-3-[[(1,2,5,6-tetrahydro-2-methyl-5,6-dioxo-1,2,4-triaz-in-3-yl)thio]methyl]-5-thia-1-aza-6R-bicyclo [4.2.O]oct-2-ene-2-pyrrolidine carboxamide-5,-dioxide) with a Ki of 0.4 μM. This inhibition is time-dependent, rapid, and only slowly reversible, with a t1/2 of 〉 3 days at 25°C. L-659, 286 is also highly selective for PMN elastase, as it does not inhibit thrombin, trypsin, papain, plasmin, chymotrypsin, or cathepsin G. L-659, 286 administered intratracheally inhibits lung damage caused by administration via the same route of human PMN elastase into hamsters. In marmosets, L-659, 286 is cleared from blood very rapidly after an intravenous injection but is recovered in bronchoalveolar lavage fluid for several hours after intratracheal administration.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240390106
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  • 3
    Electronic Resource
    Electronic Resource
    Sponge aggregation factor: In situ localization by fluorescent monoclonal antibody techniques (1986)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 31 (1986), S. 251-258 
    Details
    ISSN: 0730-2312
    Keywords: aggregation factor ; monoclonal antibodies ; reaggregation ; cell recognition ; Geodia cydonium ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The aggregation factor (AF) from sponges mediates a heterophilic interaction of homologous cells. Applying electron microscopical means, we succeeded only very rarely in identifying the 90 S AF particle in tissue sections from Geodia cydonium. By means of a fluorescent antibody technique, we have now localized the cell binding domain of the AF in situ. Previous studies in this laboratory have led to the identification of the 47-kDa cell binding protein of the AF, using the monoclonal antibody (mab) 5D2-D11 [Gramzow M, Bachmann M, Zahn RK, Uhlenbruck G, Dorn A, Müller WEG, J Cell Biol, 102:1344-1349, 1986]. This mab and mab 7D5, directed against a 92-kDa protein in the AF complex, were chosen for the fluorescent studies. By using mab 5D2-D11, the plasma membranes of cells from different regions in the sponge could be brightly stained. However, mab 7D5 reacted only very weakly with the sponge surfaces. By applying the immuno-blotting technique it was furthermore demonstrated that the cell binding protein is present both in the associated form with AF complex and in a free state. Moreover, it was established that the 47-kDa binding protein is not present in (1) homologous glycoconjugates, (2) lectin, or (3) collagen; these components are known to be involved in cell-matrix interaction.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240310402
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