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  • 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
    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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