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  • Articles: DFG German National Licenses  (3)
  • 1995-1999  (3)
  • Curing  (1)
  • PACS. 74.20.Fg BCS theory and its development - 74.72.-h High- compounds  (1)
  • immunofluorescence  (1)
Source
  • Articles: DFG German National Licenses  (3)
Material
Years
  • 1995-1999  (3)
Year
Keywords
  • 1
    Electronic Resource
    Electronic Resource
    Universal scaling in BCS superconductivity in three dimensions in non-s waves (1998)
    Springer
    The European physical journal 2 (1998), S. 31-36 
    Details
    ISSN: 1434-6036
    Keywords: PACS. 74.20.Fg BCS theory and its development - 74.72.-h High- compounds
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract: The solutions of a renormalized BCS equation are studied in three space dimensions in s, p and d waves for finite-range separable potentials in the weak to medium coupling region. In the weak-coupling limit, the present BCS model yields a small coherence length and a large critical temperature, , appropriate for some high- materials. The BCS gap, , and specific heat as a function of zero-temperature condensation energy are found to exhibit potential-independent universal scalings. The entropy, specific heat, spin susceptibility and penetration depth as a function of temperature exhibit universal scaling below in p and d waves.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100510050222
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
  • 2
    Electronic Resource
    Electronic Resource
    Regulation of cell-wall morphology and growth encoded by plasmids in Shigella dysenteriae type 1 (1995)
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 280-283 
    Details
    ISSN: 1573-0972
    Keywords: Curing ; electron microscopy ; outer membrane ; plasmids ; SDS-PAGE ; Shigella dysenteriae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Shigella dysenteriae type 1, isolated locally, was found to contain six plasmids and these could be eliminated using SDS. A 70-kb plasmid was necessary to maintain the normal cell-wall morphology. Synthesis of nine major membrane proteins (90 to 40 kDa) was severely impaired in all-plasmid cured strains. Electron microscopy revealed a prominent separation between the outer and inner membranes of the cured strains, indicating that plasmid loss led to defects in the cell envelope. The growth rates of the strains having only the 70-kb plasmid and the plasmidless strain were 3- to 30-fold less than in the wild type strain.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00367098
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Subcellular localization of IpaC, an invasion plasmid antigen of Shigella dysenteriae type 1 and its in-vitro binding capability to mammalian cells (1995)
    Springer
    World journal of microbiology and biotechnology 11 (1995), S. 578-584 
    Details
    ISSN: 1573-0972
    Keywords: HeLa cells ; immunofluorescence ; immunogold labelling ; IpaC secretion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Invasion plasmid antigen C (IpaC), a 45-kDa protein encoded by an invasion plasmid of Shigella, is associated with the invasion of epithelial cells by the bacteria. Invasive strains of S. dysenteriae type 1 secreted more proteins into the extracellular environment than a non-invasive strain and secreted more IpaC protein. An anti-IpaC mouse monoclonal antibody was used as a probe to determine the subcellular localization of IpaC and its involvement in invasion of mammalian cells. Immunogold labelling of ultrathin sections of invasive bacteria indicated that the IpaC was only present in the cytoplasmic membrane and cytoplasm. There were no gold-IgG particles on the bacterial surface. Immunoblot analysis of different cellular fractions confirmed that the protein was associated with the inner cytoplasmic membrane and cytosolic fraction. The in-vitro binding capability of the IpaC protein was assessed using HeLa and isolated rat intestinal epithelial cells. The binding of the protein to the surface of mammalian cells indicates that it may have a role in the early stages of the infection process. The binding was sensitive to the action of proteolytic enzymes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00286377
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    Paper (German National Licenses)
    Fulltext
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