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Please use this identifier to cite or link to this item: http://acervodigital.unesp.br/handle/11449/34416
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dc.contributor.authorHan, S. W.-
dc.contributor.authorMaccheroni, W.-
dc.contributor.authorRossi, A.-
dc.date.accessioned2014-05-20T15:23:40Z-
dc.date.accessioned2016-10-25T17:57:41Z-
dc.date.available2014-05-20T15:23:40Z-
dc.date.available2016-10-25T17:57:41Z-
dc.date.issued1992-01-01-
dc.identifierhttp://www.scielo.br/scielo.php?script=sci_issues&pid=0100-879X&lng=en&nrm=iso-
dc.identifier.citationBrazilian Journal of Medical and Biological Research. São Paulo: Associação Bras Divulg Cientifica, v. 25, n. 5, p. 441-447, 1992.-
dc.identifier.issn0100-879X-
dc.identifier.urihttp://hdl.handle.net/11449/34416-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/34416-
dc.description.abstract1. 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.en
dc.format.extent441-447-
dc.language.isoeng-
dc.publisherAssociação Brasileira de Divulgação Científica (ABRADIC)-
dc.sourceWeb of Science-
dc.subjectFUNGIpt
dc.subjectNEUROSPORA-CRASSApt
dc.subjectALKALINE PHOSPHATASEpt
dc.subjectENZYME SECRETIONpt
dc.subjectACID PHOSPHATASEpt
dc.subjectP-NITROPHENYLPHOSPHATEpt
dc.titleTHE PHO-2A MUTANT OF NEUROSPORA-CRASSA WHICH IS DEFICIENT IN PI-REPRESSIBLE ALKALINE-PHOSPHATASE (EC 3.1.3.1) IS ALSO DEFECTIVE IN PI-REPRESSIBLE ACID-PHOSPHATASE (EC 3.1.3.2)en
dc.typeoutro-
dc.contributor.institutionUniversidade de São Paulo (USP)-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.description.affiliationUNIV SAO PAULO,FAC FILOSOFIA CIENCIAS & LETRAS RIBEIRAO PRETO,DEPT QUIM,AV BANDEIRANTES 3900,BR-14049 RIBEIRAO PRETO,SP,BRAZIL-
dc.description.affiliationUNIV ESTADUAL PAULISTA,INST BIOCIENCIAS,DEPT BIOQUIM & MICROBIOL,BR-13500 RIO CLARO,SP,BRAZIL-
dc.description.affiliationUnespUNIV ESTADUAL PAULISTA,INST BIOCIENCIAS,DEPT BIOQUIM & MICROBIOL,BR-13500 RIO CLARO,SP,BRAZIL-
dc.identifier.wosWOS:A1992HY84800002-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofBrazilian Journal of Medical and Biological Research-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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