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  • Articles  (3)
  • alloxan-diabetes  (2)
  • Biosolubilization  (1)
  • Springer  (3)
  • American Association of Petroleum Geologists
  • 1995-1999  (1)
  • 1990-1994  (2)
  • 1905-1909
  • Biology  (3)
Collection
  • Articles  (3)
Source
Keywords
Publisher
  • Springer  (3)
  • American Association of Petroleum Geologists
Years
  • 1995-1999  (1)
  • 1990-1994  (2)
  • 1905-1909
Year
Topic
  • 1
    Electronic Resource
    Electronic Resource
    Colonization and degradation of oxidized bituminous and lignite coals by fungi (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 53-59 
    Details
    ISSN: 1476-5535
    Keywords: Bituminous coal ; Biosolubilization ; Penicillium sp. ; Surface colonization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary APenicillium sp. previously shown to grow on lignite coals degraded an air-oxidized bituminous coal (Illinois #6) to a material that was more than 80% soluble in 0.5 N NaOH. Scanning electron microscopy of the oxidized Illinois #6 revealed colonization of the surface by thePenicillium sp., production of conidia, and erosion of the coal surface. The average molecular weight (MW) of Illinois #6 degraded by the fungus and base-solubilized was approximately 1000 Da. The average MW for base-solubilized Illinois #6 that was not exposed to the fungus was 6000 Da, suggesting solubilizing mechanisms other than base catalysis. A spectrophotometric assay to quantify the microbial conversion of biosolubilized coal was developed. Standard curves were constructed based on the absorbance at 450 nm of different quantities of microbe-solubilized coal. An acid precipitation step was necessary to remove medium and/or microbial metabolites from solubilized coal to prevent overestimation of the extent of coal biosolubilization. Furthermore, the absorption spectra for different coal products varied, necessitating construction of standard curves for individual coals.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01576177
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  • 2
    Electronic Resource
    Electronic Resource
    Post-receptor defect accounts for phosphorylase hypersensitivity in cultured diabetic cardiomyocytes (1992)
    Springer
    Molecular and cellular biochemistry 117 (1992), S. 63-70 
    Details
    ISSN: 1573-4919
    Keywords: glycogen phosphorylase ; alloxan-diabetes ; cardiomyocytes ; G-protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The basis for the hypersensitive response of glycogen phosphorylase to epinephrine stimulation was investigated in adult rat cardiomyocytes isolated from normal and alloxan-diabetic animals. To assess potential G-protein involvement in the response, normal and diabetic derived myocytes were incubated with either cholera or pertussis toxin prior to hormonal stimulation. Pretreatment of cardiomyocytes with cholera toxin resulted in a potentiated response to epinephrine stimulation whereas pertussis toxin did not affect the activation of this signaling pathway. To determine if the enhanced response of phosphorylase activation resulted from an alteration in adenylate cyclase activation, the cells were challenged with forskolin. After 3 hr in primary culture, diabetic cardiomyocytes exhibited a hypersensitive response to forskolin stimulation relative to normal cells. However, after 24 hr in culture, both normal and diabetic myocytes responded identically to forskolin challenge. The present data suggest that a cholera toxin sensitive G-protein mediates the hypersensitive response of glycogen phosphorylase to catecholamine stimulation in diabetic cardiomyocytes and this response which is present in alloxan-diabetic cells and is induced in vitro in normal cardiomyocytes is primarily due to a defect at a post-receptor site.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00230411
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of the molecular basis for phosphorylase hypersensitivity in cultured diabetic cardiomyocytes (1995)
    Springer
    Molecular and cellular biochemistry 145 (1995), S. 131-139 
    Details
    ISSN: 1573-4919
    Keywords: glycogen phosphorylase ; alloxan-diabetes ; cardiomyocytes ; cGMP ; phosphodiesterase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract The focus of this study was to identify the molecular basis for the hypersensitive response of glycogen phosphorylase activation to epinephrine stimulation in alloxan diabetic-derived cardiomyocytes. Cyclic AMP levels were found not to be significantly different between normal and diabetic-derived cells while cGMP concentrations were found consistently to be significantly lower in diabetic-derived cells than in normal cells. Treatment with cyclic GMP analogues did not affect phosphorylase activation by epinephrine in normal cardiomyocytes whereas, IBMX, a nonselective phosphodiesterase inhibitor, had a significant effect on basal and agonist-stimulated phosphorylase activity in both normal and diabetic-derived cardiomyocytes. Differences in the time course for the rate of decay of phosphorylasea from agonist-stimulated to basal levels were observed between normal and diabetic cells. After 3 h in primary culture, phosphorylasea activity returned to basal levels more quickly in normal than in diabetic-derived cells while after 24 h in culture, the time for phosphorylasea decay was not significantly different between normal and diabetic myocytes and was longer than the 3 h response. After 3 h in primary culture, no significant difference in phosphorylase kinase activity was observed between normal and diabetic-derived cells exposed to epinephrine whereas, after 24 h in culture, phosphorylase kinase activity was significantly decreased in diabetic cells under basal and agonist-stimulated conditions. These data collectively suggest that the hypersensitive response of glycogen phosphorylase to epinephrine stimulation in diabetic-derived cardiomyocytes is not due to a defect present at the level of phosphorylase kinase but may, in part, result from an alteration in cardiac phosphodiesterase activity resulting from diminished intracellular cyclic GMP concentrations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00935485
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