Bovine Kidney Low Molecular Weight Acid Phosphatase: Fmn-dependent Kinetics

dc.creatorGranjeiro J.M.
dc.creatorFerreira C.V.
dc.creatorJuca M.B.
dc.creatorTaga E.M.
dc.creatorAoyama H.
dc.date1997
dc.date2015-06-30T14:49:37Z
dc.date2015-11-26T15:03:28Z
dc.date2015-06-30T14:49:37Z
dc.date2015-11-26T15:03:28Z
dc.date.accessioned2018-03-28T22:14:20Z
dc.date.available2018-03-28T22:14:20Z
dc.identifier
dc.identifierBiochemistry And Molecular Biology International. , v. 41, n. 6, p. 1201 - 1208, 1997.
dc.identifier10399712
dc.identifier
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0030976268&partnerID=40&md5=ac36a6aab0f568548dbc4296b2ce9ee8
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/100219
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/100219
dc.identifier2-s2.0-0030976268
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1256622
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 p-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.
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dc.languageen
dc.publisher
dc.relationBiochemistry and Molecular Biology International
dc.rightsfechado
dc.sourceScopus
dc.titleBovine Kidney Low Molecular Weight Acid Phosphatase: Fmn-dependent Kinetics
dc.typeArtículos de revistas


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