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  • 1
    ISSN: 1432-1890
    Keywords: Ericaceae ; Mycorrhizal fungus ; Acid invertase ; Acid phosphatase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Fractions of acid invertase and acid phosphatase of the ericoid mycorrhizal fungus Hymenoscyphus ericae (Read) Korf & Kernan were compared by column chromatography and polyacrylamide gel electrophoresis. Acid invertase levels were measured during the exponential phase after 14 days growth in pure culture. Most acid invertase was wall associated (50%) with 41% forming an extracellular fraction and 9% a soluble, cytoplasmic fraction. The wall-bound fraction was partially solubilized by 1 M NaCl, bulked with the extracellular fraction and separated by gel filtration into two acid invertase activity peaks. These peaks corresponded closely to two acid phosphatase activity peaks measured in the same eluates. Anion exchange chromatography under a continuous salt gradient separated the invertase and phosphatase isoforms from each other. Non-denaturing polyacrylamide gel electrophoresis demonstrated that the more active isoforms of each enzyme have different electrophoretic properties and are high mannose-type glycoproteins with a high affinity for the lectin, concanavalin A. The results are discussed in terms of the functional aspects of the two enzymes and their cytochemical localization.
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Mycorrhiza 6 (1996), S. 215-225 
    ISSN: 1432-1890
    Keywords: Key words Mycorrhiza ; Ericales ; Hosts ; Specificity ; Ecology
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Ericoid mycorrhiza, found in plants belonging to a few families of the Ericales, is seen as the most specific of mycorrhizas, and this has generated much research into the basis of the specificity. Recently, however, non-vascular plants have been found to be able to form the same type of mycorrhiza, and the diversity of the fungal partners has expanded. This review assesses the present state of host and ecological specificity of ericoid mycorrhizas and discusses future lines of research.
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  • 3
    ISSN: 1432-1890
    Keywords: Ericaceae ; Mycorrhizal fungi ; Acid phosphatase ; Protein expression ; Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The activity of acid phosphatase produced in pure culture by the endomycorrhizal fungus Hymenoscyphus ericae (Read) Korf & Kernan (H. ericae LPA 2) was inhibited by high phosphorus levels, alkaline pH, fluoride, molybdate and mannosidase, and activated by concanavalin A. Over 80% of the enzyme activity was due to two wall-bound acid phosphatase isozymes with the characteristics of mannose-rich glycoproteins. Antiserum was raised against the major, low-molecular-weight wall isozyme and its activity tested by immunoblotting and ELISA. The antiserum cross reacted 100% with exocellular (excreted) and 28% with cytoplasmic cellular fractions of H. ericae (LPA 2) cultures, and showed high reactivity with other strains of H. ericae but not with fungal isolates from Erica hispidula L. or E. mauritanica L. Ultrastructural localization of acid phosphatase by cytoenzymology and indirect immunogold labelling confirmed its association with the fungal wall in pure culture and showed that the influence of a high phosphorus level, fluoride and molybdate is through inactivation of the enzyme. Intense acid phosphatase activity, sensitive to the latter inhibitors, was also present on external hyphae growing over a host or non-host root but it was weak or absent from intracellular hyphae where these developed within a host root. Indirect immunolabelling confirmed that this acid phosphatase was of fungal origin and that the specific inhibitory effect of host cells is due to inactivation of the enzyme rather than repression of its synthesis. Possible implications of fungal acid phosphatase in ericoid endomycorrhizal infection processes are discussed together with mechanisms that may be regulating the enzyme activity.
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  • 4
    ISSN: 1432-1890
    Keywords: Key words Anatomy ; Ectomycorrhizas ; Morphology ; Pinus patula ; P and N utilization ; pH and temperature
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Ectomycorrhizal (ECM) fungi are an important component of the Pinus patula Schlechdt. et Cham. forest ecosystem in Mpumalanga, South Africa. ECM roots are intimately associated with accumulated litter on the forest floor and four ECM isolates where examined to determine whether they provide plant access to inorganic and organic sources of nitrogen (N) and inorganic, complexed inorganic and organic sources of phosphorus (P). In in vitro studies, all isolates were found to utilize most of the organic N compounds and organic or complexed inorganic P compounds supplied. Thus, ECM fungi could play a significant role in providing N and P to P. patula, especially from sources to which the host plant would not normally have access. Temperature sensitivities and pH optima of the four isolates differed. Of the ECM isolates WITS 01 and WITS 06 were collected from a high-litter site; WITS 01 mycorrhizas, identified as Scleroderma citrinum, were white, smooth and dichotomously branched with smooth, pale yellow, differentiated rhizomorphs. The mantle was plectenchymatous with outer and inner layers showing ring-like arrangements of hyphal bundles. The Hartig net had a palmetti shape. The WITS 02 (not identified) mycorrhizas were brown with lighter coloured root tips, with simple to dichotomous branching, smooth with no distinct mantle and sparse hyphae occurred on the root surface. The Hartig net was palmetti type with lobed haustoria. The results are discussed in relation to ECM distribution and function in nutrient cycling.
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