Purification And Kinetic Properties Of A Castor Bean Seed Acid Phosphatase Containing Sulfhydryl Groups

dc.creatorGranjeiro P.A.
dc.creatorFerreira C.V.
dc.creatorGranjeiro J.M.
dc.creatorTaga E.M.
dc.creatorAoyama H.
dc.date1999
dc.date2015-06-30T15:23:03Z
dc.date2015-11-26T15:30:01Z
dc.date2015-06-30T15:23:03Z
dc.date2015-11-26T15:30:01Z
dc.date.accessioned2018-03-28T22:38:34Z
dc.date.available2018-03-28T22:38:34Z
dc.identifier
dc.identifierPhysiologia Plantarum. , v. 107, n. 2, p. 151 - 158, 1999.
dc.identifier319317
dc.identifier10.1034/j.1399-3054.1999.100201.x
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0033405301&partnerID=40&md5=70a548e4768709f44df0762ecda82b04
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/101296
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/101296
dc.identifier2-s2.0-0033405301
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1261904
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 μkat 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 (PP(i)) as substrate. The highest specificity constant (V(max)/K(m)) was observed with PP(i), making it a potential physiological substrate.
dc.description107
dc.description2
dc.description151
dc.description158
dc.descriptionBarrett-Lennard, E.G., Robson, A.D., Greenway, H., Effect of phosphorus deficiency and water deficit on phosphatase activities from wheat leaves (1982) J Exp Bot, 33, pp. 682-693
dc.descriptionBasha, S.M., Purification and characterization of an acid phosphatase from peanut (Arachis hypogaea) seed (1984) Can J Bot, 62, pp. 385-391
dc.descriptionBiswas, T.K., Cundiff, C., Multiple forms of acid phosphatase in germinating seeds of Vigna sinensis (1991) Phytochemistry, 30, pp. 2119-2125
dc.descriptionChing, T.M., Lin, T., Metzger, R.J., Purification and properties of acid phosphatase from plump and shriveled seeds of Triticale (1987) Plant Physiol, 84, pp. 789-795
dc.descriptionConrad, F., Rüdiger, H., The lectin from pleurotus ostreatus: Purification, characterization and interaction with a phosphatase (1994) Phytochemistry, 30, pp. 277-283
dc.descriptionDuff, S.M.G., Lefebvre, D.D., Plaxton, W.C., Purification, characterization and subcellular localization of an acid phosphatase from Brassica nigra suspension cells. Comparison with phosphoenolpyruvate phosphatase (1991) Arch Biochem Biophys, 286, pp. 226-232
dc.descriptionDuff, S.M.G., Sarath, G., Plaxton, W.C., The role of acid phosphatases in plant phosphorus metabolism (1994) Physiol Plant, 90, pp. 791-800
dc.descriptionFerreira, C.V., Granjeiro, J.M., Taga, E.M., Aoyama, H., Multiple forms of soybean seeds acid phosphatases (1998) Plant Physiol Biochem, 36, pp. 487-494
dc.descriptionGellatly, K., Moorhead, G.B.G., Duff, S.M.G., Lefebvre, D.D., Plaxton, W.C., Purification and characterization of a potato tuber acid phosphatase having significant phosphotyrosine phosphatase activity (1994) Plant Physiol, 106, pp. 223-232
dc.descriptionGuo, J., Pesacreta, J.C., Purification and characterization of an acid phosphatase from the bulb of Allium cepa L., var. Sweet Spanish (1997) J Plant Physiol, 151, pp. 520-527
dc.descriptionHaraguchi, H., Yamauchi, D., Minamikawa, T., Multiple forms of acid phosphatase in cotyledons of Vigna mungo seedlings: Immunological detection and quantitation (1990) Plant Cell Physiol, 31, pp. 917-923
dc.descriptionHartree, E.F., Determination of proteins: A modification of the Lowry method that gives a linear photometric response (1972) Anal Biochem, 48, pp. 422-427
dc.descriptionHollander, V.P., Acid phosphatases (1971) The Enzymes, 4, pp. 449-498. , Boyer PD (ed) A. Academic Press, New York, NY
dc.descriptionHuyer, G., Liu, S., Kelly, J., Moffat, J., Payette, P., Kennedy, B., Tsaprailis, G., Ramachandran, C., Mechanism of inhibition of protein tyrosine phosphatase by vanadate and pervanadate (1997) J Biol Chem, 272, pp. 843-851
dc.descriptionKawarasaki, Y., Nakano, H., Yamane, T., Purification and some properties of wheat germ acid phosphatase (1996) Plant Sci, 119, pp. 67-77
dc.descriptionKruzel, M., Morawiecka, B., Acid phosphatase of potato tubers (Solanum tuberosum L.). Purification, properties, sugar and amino acid composition (1982) Acta Biochim Pol, 29, pp. 321-330
dc.descriptionLebansky, B.R., McKnight, T.D., Griffing, L.R., Purification and characterization of a secreted purple phosphatase from soybean suspension cultures (1992) Plant Physiol, 99, pp. 391-395
dc.descriptionLowry, O.H., Lopez, J.A., The determination of inorganic phosphate in the presence of labile phosphate esters (1945) J Biol Chem, 162, pp. 421-424
dc.descriptionPan, S., Characterization of multiple acid phosphatase in salt, stressed spinach leaves (1987) Aust J Plant Physiol, 14, pp. 117-124
dc.descriptionPanara, F., Pasqualini, S., Antonielli, M., Multiple forms of barley root acid phosphatase: Purification and some characteristics of the major cytoplasmic isoenzyme (1990) Biochim Biophys Acta, 1037, pp. 73-80
dc.descriptionPark, H.S.C., Van Etten, R.L., Purification and characterization of homogeneous sunflower seed acid phosphatase (1986) Phytochemistry, 25, pp. 351-357
dc.descriptionPenheiter, A.R., Duff, S.M.G., Sarath, G., Soybean root nodule acid phosphatase (1997) Plant Physiol, 114, pp. 597-604
dc.descriptionPolya, G.M., Wetlenhall, R.E.H., Rapid purification and N-terminal sequencing of a potato tuber cyclic nucleotide binding phosphatase (1992) Biochim Biophys Acta, 1159, pp. 179-184
dc.descriptionReisfeld, R.A., Lewis, V.J., Williams, D.E., Disk electrophoresis of basic proteins and peptides on polyacrylamide gels (1962) Nature, 195, pp. 281-283
dc.descriptionStaswick, P.E., Papa, C., Huang, J., Rhee, Y., Purification of the major soybean leaf acid phosphatase that is increased by seed. Pod removal (1994) Plant Physiol, 104, pp. 49-57
dc.descriptionSwarup, G., Cohen, S., Garbers, D.L., Inhibition of membrane phosphotyrosyl protein phosphate activity by vanadate (1982) Biochem Biophys Res Commun, 107, pp. 1104-1109
dc.descriptionTaga, E.M., Van Etten, R.L., Human liver acid phosphatase: Purification and properties of a low, molecular weight isoenzyme (1982) Arch Biochem Biophys, 214, pp. 505-515
dc.descriptionUllah, A.H.J., Gibson, D.M., Purification and characterization of acid phosphatase from cotyledons of germinating soybean seeds (1988) Arch Biochem Biophys, 260, pp. 514-520
dc.descriptionYumagata, H., Tanaka, K., Kasai, Z., Purification and characterization of acid phosphatase in aleurone particles of rice grains (1980) Plant Cell Physiol, 21, pp. 1449-1460
dc.descriptionYupsanis, T., Eleftheriou, P., Pantazaki, A., Georgatsos, J.G., Multiplicity of metal independent protein phosphatases of germinated alfafa seeds (1993) J Plant Physiol, 141, pp. 257-262
dc.languageen
dc.publisher
dc.relationPhysiologia Plantarum
dc.rightsfechado
dc.sourceScopus
dc.titlePurification And Kinetic Properties Of A Castor Bean Seed Acid Phosphatase Containing Sulfhydryl Groups
dc.typeArtículos de revistas


Este ítem pertenece a la siguiente institución