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  • Rhodococcus fascians  (3)
  • Acetylcholine receptor  (2)
  • Springer  (5)
  • American Association for the Advancement of Science (AAAS)
  • De Gruyter
  • 1990-1994  (5)
Collection
Keywords
Publisher
  • Springer  (5)
  • American Association for the Advancement of Science (AAAS)
  • De Gruyter
Years
  • 1990-1994  (5)
Year
  • 1
    Electronic Resource
    Electronic Resource
    Continuous limonin degradation by immobilized Rhodococcus fascians cells in K-carrageenan (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 487-493 
    Details
    ISSN: 1432-0614
    Keywords: Key words Limonin ; Debittering ; Immobilization ; Rhodococcus fascians ; Continuous Stirred Tank Reactor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Limonin can be effectively degraded by Rhodococcus fascians cells. These bacteria can be entrapped in κ-carrageenan, and used in a continuous stirred tank reactor to degrade limonin in a continuous process. The effects of temperature, limonin concentration, dilution rate, and aeration on the reactor behaviour have been tested, and the results correlated with changes in limonin conversion, substrate degradation rate, and free and immobilized biomass. Results showed that the immobilized cells were able to debitter limonin-containing media and the immobilized biomass was quite stable throughout the operational conditions tested. A population of free biomass was present in the reactor, the quantity of which was dependent on dilution rate. The immobilized bacteria increased its limonin-degrading capability when the substrate concentration was increased. The aeration was not strictly necessary for limonin degradation. Additionally, the immobilized cells were active and stable for more than 2 months of continuous operation, and were able to recover their limonin-degrading capability when used intermittently. Finally, none of the main components of a juice was noticeably altered during limonin degradation, so the reactor response was good enough to consider its application.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982541
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  • 2
    Electronic Resource
    Electronic Resource
    Continuous limonin degradation by immobilizedRhodococcus fascians cells in K-carrageenan (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 487-493 
    Details
    ISSN: 1432-0614
    Keywords: Limonin ; Debittering ; Immobilization ; Rhodococcus fascians ; Continuous Stirred Tank ; Reactor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Limonin can be effectively degraded byRhodococcus fascians cells. These bacteria can be entraped in κ-carrageenan, and used in a continuous stirred tank reactor to degrade limonin in a continuous process. The effects of temperature limonin concentration, dilution rate, and aeration on the reactor behaviour have been tested, and the results correlated with changes in limonin conversion, substrate degradation rate, and free and immobilized biomass. Results showed that the immobilized cells were able to debitter limonin-containing media and the immobilized biomass was quite stable throughout the operational conditions tested. A population of free biomass was present in the reactor, the quantity of which was dependent on dilution rate. The immobilized bacteria increased its limonin-degrading capability when the substrate concentration was increased. The aeration was not strictly necessary for limonin degradation. Additionally, the immobilized cells were active and stable for more than 2 months of continuous operation, and were able to recover their limonin-degrading capability when used intermittently. Finally, none of the main components of a juice was noticeably altered during limonin degradation, so the reactor response was good enough to consider its application.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00939041
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Continuous limonin degradation by immobilizedRhodococcus fascians cells in K-carrageenan (1994)
    Springer
    Applied microbiology and biotechnology 41 (1994), S. 487-493 
    Details
    ISSN: 1432-0614
    Keywords: Limonin ; Debittering ; Immobilization ; Rhodococcus fascians ; Continuous Stirred Tank ; Reactor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Limonin can be effectively degraded byRhodococcus fascians cells. These bacteria can be entraped in κ-carrageenan, and used in a continuous stirred tank reactor to degrade limonin in a continuous process. The effects of temperature limonin concentration, dilution rate, and aeration on the reactor behaviour have been tested, and the results correlated with changes in limonin conversion, substrate degradation rate, and free and immobilized biomass. Results showed that the immobilized cells were able to debitter limonin-containing media and the immobilized biomass was quite stable throughout the operational conditions tested. A population of free biomass was present in the reactor, the quantity of which was dependent on dilution rate. The immobilized bacteria increased its limonin-degrading capability when the substrate concentration was increased. The aeration was not strictly necessary for limonin degradation. Additionally, the immobilized cells were active and stable for more than 2 months of continuous operation, and were able to recover their limonin-degrading capability when used intermittently. Finally, none of the main components of a juice was noticeably altered during limonin degradation, so the reactor response was good enough to consider its application.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01982541
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  • 4
    Electronic Resource
    Electronic Resource
    Residues 377-389 from the δ subunit ofTorpedo californica acetylcholine receptor are located in the cytoplasmic surface (1994)
    Springer
    The protein journal 13 (1994), S. 67-76 
    Details
    ISSN: 1573-4943
    Keywords: Acetylcholine receptor ; cytoplasmic residues ; fluorophore insertion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Torpedo californica acetylcholine receptor (AcChR) enriched, sealed vesicles have been specifically labeled on the cytoplasmic surface with pyridoxal 5′-phosphate (Perez-Ramirez, B., and Martinez-Carrion, M., 1989,Biochemistry 28, 5034–5040). After chromatography of the peptide fragments produced by tryptin digestion of labeled AcChR, several fractions containing the phosphopyridoxyl label were obtained. Edman degradation identified one of the fractions, with sequence SRSELMFEKQSER, as corresponding to residues 377–389 in theδ subunit (primary structure). The latter must be a cytoplasmic region of this transmembranous protein, and residueδK385 must reside in a water-soluble exposed domain of the cytosolic side of the membrane. Introduction of phosphopyridoxyl residues allows for their potential use as probes of conformational changes in the cytosolic surface of the receptor molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01891994
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  • 5
    Electronic Resource
    Electronic Resource
    Selective labeling of α-bungarotoxin with fluorescein isothiocyanate and its use for the study of toxin-acetylcholine receptor interactions (1990)
    Springer
    The protein journal 9 (1990), S. 683-693 
    Details
    ISSN: 1573-4943
    Keywords: Acetylcholine receptor ; α-bungarotoxin ; fluorescent labels
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The main product of the reaction of fluorescein isothiocyanate (FITC) and bungarotoxin (Bgt) under near stoichiometric conditions is a monofluorescein derivative preferentially labeled at Lys 26, a highly conserved residue known to be involved in the binding (McDaniel, C. S., Manshouri, T., and Atassi, M. Z. (1987)J. Prot. Chem. 6, 455–461; Garcia-Borron, J. C., Bieber, A. L., and Martinez-Carrion, M. (1987)Biochemistry 26, 4295–4303) of postsynaptic neurotoxins specific for the nicotinic acetylcholine receptor (AcChR). The fluorescently labeled toxin retains a high affinity for the AcChR, and an unaltered specificity. Binding of FITC-Bgt to AcChR results in a significant decrease in the fluorescence intensity of the probe. This AcChR-mediated quenching of FITC-Bgt fluorescence allows for a continuous monitoring of the binding process. The quenching of free and bound FITC-Bgt by charged and neutral quenchers shows few fluorophore accessibility changes as induced by the toxin-bound state. The results are consistent with a model in which the positively charged concave surface of the toxin interacts with a negatively charged complementary surface in the receptor molecule.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01024763
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