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  • 1995-1999  (3)
  • Glomus fasciculatum  (1)
  • IpaC secretion  (1)
  • PACS. 71.23.Ft Quasicrystals - 61.44.-n Semi-periodic solids  (1)
  • 1
    ISSN: 1573-5036
    Keywords: Bombyx mori ; Glomus fasciculatum ; Glomus mosseae ; Morus alba ; phosphorus uptake VA-mycorrhiza
    Source: Springer Online Journal Archives 1860-2000
    Topics: Agriculture, Forestry, Horticulture, Fishery, Domestic Science, Nutrition
    Notes: Abstract A field experiment was conducted for four years with Kanva-2 variety of mulberry, pre-inoculated with Glomus fasciculatum and Glomus mosseae at various doses of single super phosphate to examine their effect on plant growth, leaf yield and quality. The pooled data for 4 years revealed that the effect of inoculation of mulberry with Glomus mosseae in combination with 30 kg P ha-1 yr-1 was similar for plant growth, leaf yield and leaf chemical constituents with the control, which received the full dose of phosphatic fertilizer (120 kg P ha-1 yr-1) without inoculation. This indicated a possibility to reduce phosphate fertilization in mulberry cultivation by 75%. Silkworm rearing (moulting test) also did not reveal any significant difference in the leaf quality even after reducing phosphorus application by 75% in mulberry inoculated with either Glomus mosseae or Glomus fasciculatum when compared with control. The root colonization was significantly higher in VAM inoculation at the lower levels of phosphorus compared to uninoculated control receiving the full dose of phosphate fertilizer (120 kg P ha-1 yr-1) suggesting that low phosphorus levels in soil promote better VA-mycorrhizal symbiosis in mulberry.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    The European physical journal 11 (1999), S. 575-582 
    ISSN: 1434-6036
    Keywords: PACS. 71.23.Ft Quasicrystals - 61.44.-n Semi-periodic solids
    Source: Springer Online Journal Archives 1860-2000
    Topics: Physics
    Notes: Abstract: We present an exact real-space renormalization group (RSRG) scheme for the electronic Green's functions of one-dimensional tight-binding systems having both nearest-neighbor and next-nearest-neighbor hopping integrals, and determine the electronic density of states for the quasiperiodic Fibonacci chain. This RSRG method also gives the Lyapunov exponents for the eigenstates. The Lyapunov exponents and the analysis of the flow pattern of hopping integrals under renormalization provide information about the nature of the eigenstates. Next we develop a transfer matrix formalism for this generalized tight-binding system, which enables us to determine the wave function amplitudes. Interestingly, we observe that like the nearest-neighbor tight-binding Fibonacci chain, the present generalized tight-binding system also have critical eigenstates, Cantor-set energy spectrum and highly fragmented density of states. It indicates that these exotic physical properties are really the characteristics of the underlying quasiperiodic structure.
    Type of Medium: Electronic Resource
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  • 3
    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
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