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  • chick embryonic muscle  (1)
  • fungi  (1)
  • 1990-1994  (2)
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  • 1990-1994  (2)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Comparison of coal solubilization by bacteria and fungi (1994)
    Springer
    Biodegradation 5 (1994), S. 55-62 
    Details
    ISSN: 1572-9729
    Keywords: ammonia ; bacteria ; chelation ; coal solubilization ; fungi ; oxalate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract Coal-solubilizing agents produced byTrametes versicolor, Phanerochaete chrysosporium, Aspergillus sp., a bacterial consortium, and a bacterial isolate,Arthrobacter sp., from that consortium were compared in terms of pH dependence, thermostability, molecular mass, mechanism of action, and product diversity. The thermostability and low molecular weights exhibited by the coal-solubilizing agents indicated a non-enzymatic mechanism of action. Competition studies using cupric copper indicated that coal solubilization by these agents involved metal chelation. Results demonstrated that oxalate could account for some but not all of the coal solubilization observed forT.versicolor andP.chrysosporium. The very low levels of oxalate detected inAspergillus sp. and the bacterial cultures indicated that oxalate is not an important factor in coal solubilization by these microbes. When subjected to gel permeation chromatography, the soluble coal products generated by each microbial coal-solubilizing agent yielded unique molecular mass profiles suggesting substantial product diversity. Such diversity increases the possibility of identifying potentially valuable compounds and extending the commercial utilization of coal.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00695214
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  • 2
    Electronic Resource
    Electronic Resource
    Calcium influxes and calmodulin modulate the expression and physicochemical properties of acetylcholinesterase molecular forms during developmentin vivo (1993)
    Springer
    Cellular and molecular neurobiology 13 (1993), S. 217-232 
    Details
    ISSN: 1573-6830
    Keywords: acetylcholinesterase ; depolarization ; intracellular Ca2+ ; calmodulin ; chick embryonic muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary 1. Acetylcholinesterase (AcChoE; EC 3.1.1.7) exists in several molecular forms that may be anchored to cell membranes or associated with extracellular matrix. AcChoE bound to lipidic membranes is detergent extractable (DE AcChoE), whereas the enzyme associated with extracellular matrix is high salt soluble (HSS AcChoE). The latter variant is accumulated insynaptic regions by an unknown mechanism. 2. We have suggested previously that depolarization-induced Ca2+ influx is a major factor that modulates AcChoE synthesisin vivo, as well as the conversion of some DE AChoE to HSS variant. In the present study, we have examined (i) the effects of depolarization-induced skeletal muscle inactivity and ionophore-induced Ca2+ influxes on the expression of AcChoE molecular forms and (ii) the hypothesis that Ca2+-dependent calmodulin may be involved in the conversion of at least some forms of DE AcChoE to HSS variantin vivo. 3. Chick embryos were treatedin ovo during the early period of nervemuscle interactions withd-tubocurarine (dTC; a competitive neuromuscular blocking agent) or with decamethonium (dMET; a depolarizing agent). Both dTC and dMET equally and significantly reduced embryonic neuromuscular activity (motility). However, dTC significantly decreased AcChoE overall activity, whereas dMET had virtually no effect on AcChoE expression, compared to controls. 4. Treatment of embryos with the Ca2+ ionophore A23187 significantly increased the total AcChoE activity as well as the DE/HSS ratio of each AcChoE molecular form. However, treatment with N-(6-Aminohexyl)-5-chloro-1-naphthalenesulfonamide (also termed W-7), a calmodulin antagonist, did not alter the total AcChoE activity, but significantly increased the DE/HSS ratio of AcChoE forms. 5. These results support the idea that (i) depolarization and/or Ca2+ influxes, but not muscle contraction, may regulate AcChoE expression in skeletal muscle and (ii) Ca2+-dependent calmodulin activation may be involved in the conversion of some DE AcChoE to their HSS variantin vivo.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00733751
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