Han, S. W.Maccheroni, W.Rossi, A.2014-05-202014-05-201992-01-01Brazilian Journal of Medical and Biological Research. São Paulo: Associação Bras Divulg Cientifica, v. 25, n. 5, p. 441-447, 1992.0100-879Xhttp://hdl.handle.net/11449/344161. The mycelial Pi-repressible acid phosphatase presented p-nitrophenylphosphatase activity with negative cooperativity and Michaelian behavior when synthesized by the wild-type and pho-2A mutant strains of Neurospora crassa, respectively.2. The major acid phosphatase present in cell extracts of the pho-2A mutant of N. crassa grown in low Pi medium is more thermolabile (t1/2 = 4 min at 54-degrees-C, pH 5.4) than that of the wild strain (stable for at least 80 min at 54-degrees-C, pH 5.4).3. The pho-2A mutant of N. crassa secreted a more thermolabile acid phosphatase (t1/2 = 30 min at 50-degrees-C, pH 5.4) than the wild strain (t1/2 of at least 80 min at 50-degrees-C, pH 5.4).4. The pho-2A mutant of N. crassa synthesized a more thermolabile acid phosphatase (t1/2 = 37 min at 54-degrees-C, pH 5.4) than the wild strain in high Pi medium (t1/2 = 14 min al 54-degrees-C, pH 5.4).5. The pleiotropic nature of the pho-2 locus and its possible involvement in the mechanism of phosphatase secretion by N. crassa are proposed.441-447engFUNGINEUROSPORA-CRASSAALKALINE PHOSPHATASEENZYME SECRETIONACID PHOSPHATASEP-NITROPHENYLPHOSPHATEArtigoWOS:A1992HY84800002Acesso restrito