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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 dry weight. The ecto-ATPase activity was increased at about five times (498.3 ± 27.6 nmol Pi h −1 mg −1 ) in the presence of 5 mM MgCl 2 , with values of V max and apparent K m for Mg-ATP 2− corresponding to 541.9 ± 48.6 nmol Pi h −1 mg −1 cellular dry weight and 1.9 ± 0.2 mM, respectively. The Mg 2+ -stimulated ecto-ATPase activity was insensitive to inhibitors of intracellular ATPases such as vanadate (P-ATPases), bafilomycin A 1 (V-ATPases) , and oligomycin (F-ATPases). Inhibitors of acid phosphatases (molybdate, vanadate, and fluoride) or alkaline phosphatases (levamizole) had no effect on the ecto-ATPase activity. The surface of the Mg 2+ -stimulated ATPase in F. pedrosoi was confirmed by assays in which 4,4′-diisothiocyanostylbene-2,2′-disulfonic acid (DIDS), a membrane impermeant inhibitor, and suramin, an inhibitor of ecto-ATPase and antagonist of P 2 purinoreceptors. Based on the differential expression of ecto-ATPases in the different morphological stages of F. pedrosoi , the putative role of this enzyme in fungal biology is discussed.
Archives of Microbiology – Springer Journals
Published: Jun 1, 2006
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