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  • 1
    Electronic Resource
    Electronic Resource
    Base stacking in A fluorescent dinucleoside monophosphate: εApεA (1978)
    New York : Wiley-Blackwell
    Biopolymers 17 (1978), S. 1361-1372 
    Details
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The optical properties of the 1,N6 - etheno derivative of ApA (εApεA) have been studied. Absorbance and CD measurements suggest that (1) neutral salts tend to unstack this molecule and (2) the stacking interaction is weaker than in ApA. εApεA is found to be quenched strongly with respect to the monomer. (εAMP); this quenching is solvent dependent (1M NaCl 〉 5M NaClo4〉40%glycerol) and increases with the ratio of temperature to viscosity (T/η) in each case. Fluorescence lifetime measurements also reveal a temperature- and solvent-dependent decay which is nonlinear on a semilog plot. In the presence of 95% glycerol, this decay return to linearity. These data have been considered from two points of view: (1) two-state pictures which are based on thermodynamic least-squares fit to quatum yield and CD curves, together with two exponential fits to the decay curves and (2) a dynamical model in which relatives fluorophore motion leads to deexcitation via intramolecular collision. A simple model of type (2) gives qualitative agreement with the observed behavior.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bip.1978.360170519
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  • 2
    Electronic Resource
    Electronic Resource
    Design, construction, and operation of some all-glass pilot-plant fermetors (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1345-1375 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The design, Construction, and operation of a 400 liter all-glass fermentor, made from industrial glass Components, is described in detail. Outline details are also given for 100 and liter vessels of similar construction. The performance of the 400 liter fermentor with a variety of organisms is discussed. Harvesting performance. Using a disk-stak centrifuge, is also described.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260200904
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  • 3
    Electronic Resource
    Electronic Resource
    Controlled drug release by polymer dissolution. I. Partial esters of maleic anhydride copolymers - properties and theory (1978)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 22 (1978), S. 1991-2009 
    Details
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: The kinetics of drug release from a series of partial esters of vinyl acetate-maleic anhydride has been investigated. These polymers in their un-ionized forms are hydrophobic and water insoluble, but in their ionized forms they are water soluble. Polymer dissolution is pH sensitive, and different half-esters have a characteristic pH range above which they are soluble and below which they are insoluble. When films are placed in buffered media, they erode at a constant rate that depends on the pH of dissolution of the polymer and on the pH of the buffered medium. Dissolution of the polymer is limited to the polymer-buffer medium interface, and drugs dissolved or uniformly dispersed in the polymer are released by zero-order kinetics. A detailed model has been developed that successfully correlates dissolution behavior and various experimental parameters.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/app.1978.070220720
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  • 4
    Electronic Resource
    Electronic Resource
    Glucocorticoid-mediated alteration in growth factor binding and action: Analysis of the binding change (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 9 (1978), S. 69-77 
    Details
    ISSN: 0091-7419
    Keywords: dexamethasone ; epidermal growth factor ; human diploid fibroblasts ; cell proliferation ; permissive effect ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The addition of the glucocorticoid analog dexamethasone (DX) to serum-free cultures of human fibroblasts caused a twofold enhancement of the mitogenic response to epidermal growth factor (EGF), although DX by itself was not mitogenic. A basis for this effect was suggested by studies showing that DX also increased the cellular binding of 125I-EGF. DX increased the ability of the cells to bind 125I-EGF only at low physiological concentrations of this polypeptide. Thus, data from 125I-EGF binding to cells incubated without DX produced a linear Scatchard plot, whereas the data from 125I-EGF binding to DX-treated cells led to an upwardly curvilinear Scatchard plot. Measurements of 125I-EGF association with the cell surface and cytoplasm indicated that this binding change involved an alteration of cell surface EGF receptors. The binding change appeared not to involve negatively cooperative interactions between EGF receptors, nor a change in the number of receptors. The binding alteration could be explained by a model in which DX converted 25-30% of the cell surface EGF receptors to a form having a fourfold increased affinity.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400090108
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  • 5
    Electronic Resource
    Electronic Resource
    Inhibition by protease inhibitors of binding of adrenal and sex steroid hormones (1978)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 9 (1978), S. 421-426 
    Details
    ISSN: 0091-7419
    Keywords: aldosterone ; dexamethasone ; dihydrotestosterone ; estrogen ; progesterone ; steroid hormone receptor ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Binding of steroid hormones is inhibited by protease inhibitors and substrates. The protease inhibitors phenylmethyl sulphonylfluoride, tosyl-lysine chloromethyl ketone, and tosylamide-phenylethyl-chloromethyl ketone and the protease substrates tosyl arginine methyl ester and tryptophan methyl ester eliminate specific binding of aldosterone, dexamethasone, dihydrotestosterone, estrogen, and progesterone to their respective receptors. These protease inhibitors and substrates also inhibit binding of progesterone to the 20,000 molecular weight mero-receptor formed from the progesterone receptor in chick oviduct. The binding of estradiol to rat alpha-fetoprotein is inhibited by the protease inhibitors and substrates but not by tryptophan or tryptophan amide, indicating the importance of an ester structure in the inhibition of steroid binding. Our results suggest that all steroid hormone receptors have a site with both common structural features and a role in the regulation of steroid hormone binding.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400090312
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