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  • Articles  (3)
  • dexamethasone  (2)
  • catalase  (1)
  • Wiley-Blackwell  (3)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Springer Nature
  • 1975-1979  (3)
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  • Articles  (3)
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  • Wiley-Blackwell  (3)
  • American Chemical Society
  • American Institute of Physics (AIP)
  • Springer Nature
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  • 1
    Electronic Resource
    Electronic Resource
    An electron microscopic and enzymic study of rat liver peroxisomal nucleoid core and its association with urate oxidase (1977)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 7 (1977), S. 419-434 
    Details
    ISSN: 0091-7419
    Keywords: peroxisome ; microbody ; nucleoid core ; urate oxidase ; starvation effects ; rat liver enzymes ; catalase ; cell organelle ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The appearance of the characteristic crystalloid core of rat liver peroxisomes is emulated by the electron microscopic (EM) appearance of highly purified urate oxidase prepared from the same tissue. The purity of the enzyme preparation was established by gel electrophoresis under various conditions and the specific enzyme activity was at least as high as any previously reported. The amino acid composition of urate oxidase was determined. As additional evidence for close association of the peroxisomal core with urate oxidase, it was demonstrated that the biphasic changes in rat liver urate oxidase activity in response to prolonged starvation were paralleled by changes in the EM appearance of peroxisomes. Under comparable conditions catalase, another peroxisomal enzyme, did not show the same changes in activity as did urate oxidase. Evidence for the possible identity of urate oxidase with the peroxisomal crystalloid of rat liver has been presented, all materials having been obtained from, and experiments performed with, the rat.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400070313
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  • 2
    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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  • 3
    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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