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  • Articles  (4)
  • glycogen phosphorylase  (2)
  • Biocontrol of snails  (1)
  • Calcium uptake  (1)
  • Springer  (4)
  • American Association of Petroleum Geologists
  • 1995-1999  (1)
  • 1990-1994  (3)
  • 1905-1909
  • Biology  (4)
Collection
  • Articles  (4)
Source
Keywords
Publisher
  • Springer  (4)
  • American Association of Petroleum Geologists
Years
  • 1995-1999  (1)
  • 1990-1994  (3)
  • 1905-1909
Year
Topic
  • 1
    Electronic Resource
    Electronic Resource
    Fermentation and toxin studies of the molluscicidal strains ofBacillus brevis (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 112-119 
    Details
    ISSN: 1476-5535
    Keywords: MolluscicidalBacillus toxin ; Bacillus brevis ; Biomphalaria glabrata ; Biocontrol of snails ; Antioxidant preservation of toxin ; Secondary fermentation factor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Strain SS86-4 was one of 40Bacillus brevis strains shown to be molluscicidal to the schistosomiasis snail vectorBiomphalaria glabrata. When grown in mB4 medium in 2-L fermentors, SS86-4 was molluscicidal only if fructose or phenylalanine was present in the medium. This is reminiscent of secondary fermentation factor effects, in this case an antioxidant effect. In vivo proteases also were capable of reducing molluscicidal activity. The molluscicidal toxin has an LC50 of 1 μg toxin protein ml−1 (approx. 1 p.p.m.) and may be described as a small proteinaceous, heat-stable, oxygen-sensitive entity associated with the particulate portion of the cell wall fraction ofB. brevis that is formed prior to sporulation. Initial information indicates that its HPLC signature shows major peaks at 148.37 and 163.96 s and consists of two bands of approximately 5.3 kDa and 8.7 kDa on PAGE gel.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01584108
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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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  • 4
    Electronic Resource
    Electronic Resource
    Al3+-Ca2+ interactions in aluminum rhizotoxicity (1993)
    Springer
    Planta 192 (1993), S. 98-103 
    Details
    ISSN: 1432-2048
    Keywords: Aluminum toxicity ; Calcium uptake ; Growth inhibition ; Root ; Triticum
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The cation Al3+ is toxic to plants at micromolar concentrations and can severely inhibit root growth in solution experiments. Trivalent aluminum hydrolyzes in solution, and, apart from the Al3+ ion, which dominates speciation below pH 5.0, various mononuclear and polynuclear hydroxy-Al species can also occur (Kinraide 1991). Accumulating evidence suggests that Al3+ is the rhizotoxic species under the experimental conditions used in the present study (Kinraide 1991; Kinraide et al. 1992). The inhibition of Ca2+ uptake in roots by Al3+ has been proposed as a possible mechanism for Al3+ toxicity, and in this study the hypothesis was tested directly. Root growth and Ca2+ uptake were measured in 5-d-old seedlings of wheat (Triticum aestivum L. Thell) during exposure to Al3+ in a low-Ca2+ basal medium, and to Al3+ in the presence of added cations. Uptake of Ca2+ in whole roots and translocation to the shoot were measured using 45Ca2+, and localized measurements of net Ca2+ flux were also made at the root apex using the technique of microelectrode ion-flux estimation. Treatment with 2.64 μM AlCl3 in 226 μM CaCl2, at pH 4.5, severely inhibited root growth without affecting Ca2+ uptake. Addition of 30 mM Na2+, 3 mM Mg2+ or 50 μM tris(ethylenediamine)cobalt(III) to this Al3+ treatment restored root growth but significantly reduced Ca2+ uptake measured over the entire root system and at the root apex. The Al3+ and Ca2+ concentrations were adjusted so that the activities of the Al3+ and Ca2+ ions were constant in all solutions (1.5 μM and 200 μM, respectively). Root growth can be severely inhibited by Al3+ concentrations that do not affect Ca2+ uptake, while the addition of ameliorating cations depresses Ca2+ uptake. These results argue against the hypothesis that Al3+ inhibits root growth by reducing Ca2+ uptake.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00198698
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