Purification and kinetic proper ties of a castor bean seed acid phosphatase containing sulfhydryl groups

dc.creatorGranjeiro, PA
dc.creatorFerreira, CV
dc.creatorGranjeiro, JM
dc.creatorTaga, EM
dc.creatorAoyama, H
dc.date1999
dc.dateOCT
dc.date2014-12-02T16:29:01Z
dc.date2015-11-26T16:38:20Z
dc.date2014-12-02T16:29:01Z
dc.date2015-11-26T16:38:20Z
dc.date.accessioned2018-03-28T23:21:38Z
dc.date.available2018-03-28T23:21:38Z
dc.identifierPhysiologia Plantarum. Munksgaard Int Publ Ltd, v. 107, n. 2, n. 151, n. 158, 1999.
dc.identifier0031-9317
dc.identifierWOS:000084245500001
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/58463
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/58463
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/58463
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1272242
dc.descriptionAn acid phosphatase (EC 3.1.3.2) has been identified and purified from castor bean (Ricinus communis L., IAC-80) seed through sulphopropyl (SP)-Sephadex, diethylaminoethyl (DEAE)-Sephadex, Sephacryl S-200, and Concanavalin A-Sepharose chromatography. The enzyme was purified 2000-fold to homogeneity, with a final specific activity of 3.8 mu kat mg(-1) protein. The purified enzyme revealed a single diffuse band with phosphatase activity on nondenaturing polyacrylamide gel electrophoresis, at pH 8.3. The relative molecular mass, determined by high-performance liquid chromatography (HPLC), was found to be 60 kDa, The acid phosphatase had a pH optimum of 5.5 and an apparent K-m value for p-nitrophenylphosphate of 0.52 mM, The enzyme-catalyzed reaction was inhibited by inorganic phosphate, fluoride, vanadate, molybdate, p-chloromercuribenzoate (pCMB), Cu2+ and Zn2+, The strong inhibition by pCMB, Cu2+ and vanadate suggests the presence of sulfhydryl groups essential for catalysis. The castor bean enzyme also recognized tyrosine-phosphate and inorganic pyrophosphate (PPi) as substrate. The highest specificity constant (V-max/K-m) was observed with PPi, making it a potential physiological substrate.
dc.description107
dc.description2
dc.description151
dc.description158
dc.languageen
dc.publisherMunksgaard Int Publ Ltd
dc.publisherCopenhagen
dc.publisherDinamarca
dc.relationPhysiologia Plantarum
dc.relationPhysiol. Plant.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectMultiple Forms
dc.subjectSuspension-cultures
dc.subjectProtein
dc.subjectCotyledons
dc.subjectInhibition
dc.subjectIsoenzyme
dc.subjectVanadate
dc.subjectLeaves
dc.titlePurification and kinetic proper ties of a castor bean seed acid phosphatase containing sulfhydryl groups
dc.typeArtículos de revistas


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