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chromoblastomycosis/phosphatase

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Phosphatase activity on the cell wall of Fonsecaea pedrosoi.

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The activity of a phosphatase was characterized in intact mycelial forms of Fonsecaea pedrosoi, a pathogenic fungus that causes chromoblastomycosis. At pH 5.5, this fungus hydrolyzed p-nitrophenylphosphate (p-NPP) to p-nitrophenol (p-NP) at a rate of 12.78 +/- 0.53 nmol p-NP per h per mg hyphal dry

Surface phosphatase in Rhinocladiella aquaspersa: biochemical properties and its involvement with adhesion.

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Rhinocladiella aquaspersa is an etiologic agent of chromoblastomycosis, a subcutaneous chronic infectious disease. In the present work, we found that the three morphological forms of this fungus (conidia, mycelia and sclerotic bodies) expressed different levels of ecto-phosphatase activity. Our

Characterization of an ecto-ATPase activity in Fonsecaea pedrosoi.

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In this work, we characterized an ecto-ATPase activity in intact mycelial forms of Fonsecaea pedrosoi, the primary causative agent of chromoblastomycosis. In the presence of 1 mM EDTA, fungal cells hydrolyzed adenosine-5'-triphosphate (ATP) at a rate of 84.6 +/- 11.3 nmol Pi h(-1) mg(-1) mycelial

Differentiation of Fonsecaea pedrosoi mycelial forms into sclerotic cells is induced by platelet-activating factor.

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Platelet-activating factor (PAF) has been shown to induce the differentiation of several cell types. In this work, we evaluated the effects of PAF on the formation of sclerotic cells of Fonsecaea pedrosoi, the major causative agent of chromoblastomycosis. Cell differentiation was evaluated by light
A cell-wall-associated phosphatase in hyphae of Fonsecaea pedrosoi, a fungal pathogen causing chromoblastomycosis, was previously characterized by the authors. In the present work, the expression of an acidic ectophosphatase activity in F. pedrosoi conidial forms was investigated. The surface
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