dc.creatorGranjeiro, JM
dc.creatorFerreira, CV
dc.creatorJuca, MB
dc.creatorTaga, EM
dc.creatorAoyama, H
dc.date1997
dc.dateMAY
dc.date2014-12-16T11:37:39Z
dc.date2015-11-26T16:26:40Z
dc.date2014-12-16T11:37:39Z
dc.date2015-11-26T16:26:40Z
dc.date.accessioned2018-03-28T23:07:31Z
dc.date.available2018-03-28T23:07:31Z
dc.identifierBiochemistry And Molecular Biology International. Academic Press Aust, v. 41, n. 6, n. 1201, n. 1208, 1997.
dc.identifier1039-9712
dc.identifierWOS:A1997WZ27600015
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/78236
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/78236
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/78236
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1268960
dc.descriptionA low molecular weight bovine kidney acid phosphatase, electrophoretically homogeneous and with a relative molecular mass of 17.8 kDa, was used in this work. Among the various substrates tested, FMN was found to be the most effective, at pH 7.0. Distinct activation energy values were obtained for nitrophenyl phosphate- (45.44 kJ mol(-1)) and flavin mononucleotide- (28.60 kJ mol-1) hydrolysis reactions. The FMN hydrolysis was strongly inhibited by Cu2+ and pCMB, but activated by guanosine. Pyridoxal-phosphate and vanadate were competitive inhibitors for the FMN-dependent reaction.
dc.description41
dc.description6
dc.description1201
dc.description1208
dc.languageen
dc.publisherAcademic Press Aust
dc.publisherMarrickville
dc.publisherAustralia
dc.relationBiochemistry And Molecular Biology International
dc.relationBiochem. Mol. Biol. Int.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectacid phosphatase
dc.subjectFMN kinetics
dc.subjecteffectors
dc.subjectactivation energy
dc.subjectPhosphotyrosine Protein Phosphatase
dc.subjectPurification
dc.subjectHeart
dc.titleBovine kidney low molecular weight acid phosphatase: FMN-dependent kinetics.
dc.typeArtículos de revistas


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