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Volumn 23, Issue 1, 2010, Pages 93-98

Effect of copper on the activation of the acid phosphatase from the green algae Pseudokirchneriella subcapitata

Author keywords

Enzyme; Fungicide; Metal; Phytoplankton; Selenastrum capricornutum; Toxicity

Indexed keywords

ACID PHOSPHATASE; COPPER;

EID: 77949424855     PISSN: 09660844     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10534-009-9270-z     Document Type: Article
Times cited : (7)

References (44)
  • 1
    • 0037005954 scopus 로고    scopus 로고
    • Copper and cadmium increase laccase activity in Pleurotus ostreatus
    • doi:10.1111/j.1574-6968.2002.tb10988.x
    • Baldrian P, Gabriel J (2002) Copper and cadmium increase laccase activity in Pleurotus ostreatus. FEMS Microbiol Lett 206:69-74. doi:10.1111/j.1574-6968. 2002.tb10988.x.
    • (2002) FEMS Microbiol Lett , vol.206 , pp. 69-74
    • Baldrian, P.1    Gabriel, J.2
  • 2
    • 0014020602 scopus 로고
    • Properties of the induced acid phosphatase and of the constitutive acid phosphatase of Euglena
    • Bennum A, Blum JJ (1966) Properties of the induced acid phosphatase and of the constitutive acid phosphatase of Euglena. Biochim Biophys Acta 128:106-123.
    • (1966) Biochim Biophys Acta , vol.128 , pp. 106-123
    • Bennum, A.1    Blum, J.J.2
  • 3
    • 0030272166 scopus 로고    scopus 로고
    • Toxicology of cupric salts on honeybees. V. Gluconate and sulfate action on gut alkaline and acid phosphatases
    • doi:10.1006/eesa.1996.0082
    • Bounias M, Kruk I, Nectoux M, Popeskovic D (1996) Toxicology of cupric salts on honeybees. V. Gluconate and sulfate action on gut alkaline and acid phosphatases. Ecotoxicol Environ Saf 35:67-76. doi:10.1006/eesa.1996.0082.
    • (1996) Ecotoxicol Environ Saf , vol.35 , pp. 67-76
    • Bounias, M.1    Kruk, I.2    Nectoux, M.3    Popeskovic, D.4
  • 4
    • 0016838369 scopus 로고
    • Ultrastructural localization of phosphohydrolases in gametes, zygotes and zoospores of Ulva mutabilis FØYN
    • Braten T (1975) Ultrastructural localization of phosphohydrolases in gametes, zygotes and zoospores of Ulva mutabilis FØYN. J Cell Sci 17:647-653.
    • (1975) J Cell Sci , vol.17 , pp. 647-653
    • Braten, T.1
  • 5
    • 0014817633 scopus 로고
    • Purification and properties of an acid phosphatase from bovine brain
    • doi:10.1016/0003-9861(70)90039-1
    • Chaimovich H, Nome F (1970) Purification and properties of an acid phosphatase from bovine brain. Arch Biochem Biophys 139:9-16. doi:10.1016/0003-9861(70)90039-1.
    • (1970) Arch Biochem, Biophys , vol.139 , pp. 9-16
    • Chaimovich, H.1    Nome, F.2
  • 6
    • 0016268615 scopus 로고
    • The properties and subcellular localization of acid phosphatases in the colourless alga Polytomella caeca
    • Cooper A, Bowen ID, Lloyd D (1974) The properties and subcellular localization of acid phosphatases in the colourless alga Polytomella caeca. J Cell Sci 15:605-618.
    • (1974) J Cell Sci , vol.15 , pp. 605-618
    • Cooper, A.1    Bowen, I.D.2    Lloyd, D.3
  • 7
    • 0004262303 scopus 로고
    • 3rd edn. Longmans Green and Co Ltd. London
    • Dixon M, Webb EC (1979) Enzymes, 3rd edn. Longmans Green and Co Ltd., London.
    • (1979) Enzymes
    • Dixon, M.1    Webb, E.C.2
  • 8
    • 0026589122 scopus 로고
    • Pseudomonas aeruginosa acid phosphatase: Activation by divalent cations and inhibition by aluminium ions
    • doi:10.1016/0014-5793(92)80108-S
    • Domenich CEA, Teresita AL, Salvano MA et al (1992) Pseudomonas aeruginosa acid phosphatase: activation by divalent cations and inhibition by aluminium ions. FEBS Lett 299:96-98. doi:10.1016/0014-5793(92)80108-S.
    • (1992) FEBS Lett , vol.299 , pp. 96-98
    • Domenich, C.E.A.1    Teresita, A.L.2    Salvano, M.A.3
  • 9
    • 0013690513 scopus 로고
    • The endomembrane system and mechanism of membrane flow in the green alga, Gloeomonas kupfferi (Volvocales, Chlorophyta) II. A cytochemical analysis
    • doi:10.1007/BF0132 2983
    • Domozych DS (1989) The endomembrane system and mechanism of membrane flow in the green alga, Gloeomonas kupfferi (Volvocales, Chlorophyta) II. A cytochemical analysis. Protoplasma 149:108-119. doi:10.1007/BF0132 2983.
    • (1989) Protoplasma , vol.149 , pp. 108-119
    • Domozych, D.S.1
  • 10
    • 0035174440 scopus 로고    scopus 로고
    • Development of flow cytometry-based algal bioassays for assessing toxicity of copper in natural waters
    • doi:10.1897/1551-5028(2001)020\0160:DOFCBA[ 2.0.CO;2
    • Franklin NM, Stauber JL, Lim RP (2001) Development of flow cytometry-based algal bioassays for assessing toxicity of copper in natural waters. Environ Toxicol Chem 20:160- 170. doi:10.1897/1551-5028(2001)020\0160: DOFCBA[ 2.0.CO;2.
    • (2001) Environ Toxicol Chem , vol.20 , pp. 160-170
    • Franklin, N.M.1    Stauber, J.L.2    Lim, R.P.3
  • 12
    • 0026668489 scopus 로고
    • Short and long term effects of copper on the rosby barb (Puntius conchonius Ham)
    • doi:10.1016/0147- 6513(92)90079-I
    • Gill TS, Tewari H, Pande J (1992) Short and long term effects of copper on the rosby barb (Puntius conchonius Ham). Ecotoxicol Environ Saf 23:294-306. doi:10.1016/0147- 6513(92)90079-I.
    • (1992) Ecotoxicol Environ Saf , vol.23 , pp. 294-306
    • Gill, T.S.1    Tewari, H.2    Pande, J.3
  • 13
    • 0030976268 scopus 로고    scopus 로고
    • Bovine kidney low molecular weight acid phosphatase: FMNdependent kinetics
    • Granjeiro JM, Ferreira CV, Juca MB et al (1997) Bovine kidney low molecular weight acid phosphatase: FMNdependent kinetics. Biochem Mol Biol Int 41:1201-1208.
    • (1997) Biochem Mol Biol Int , vol.41 , pp. 1201-1208
    • Granjeiro, J.M.1    Ferreira, C.V.2    Juca, M.B.3
  • 14
    • 0033405301 scopus 로고    scopus 로고
    • Purification and kinetic properties of a castor bean seed acid phosphatase
    • doi:10.1034/j.1399-3054.1999.100201.x
    • Granjeiro PA, Ferreira CV, Granjeiro JM et al (1999) Purification and kinetic properties of a castor bean seed acid phosphatase. Physiol Plant 107:151-158. doi:10.1034/j.1399-3054.1999.100201.x.
    • (1999) Physiol Plant , vol.107 , pp. 151-158
    • Granjeiro, P.A.1    Ferreira, C.V.2    Granjeiro, J.M.3
  • 15
    • 0036236775 scopus 로고    scopus 로고
    • Effect of copper on algal communities fromoligotrophic calcareous streams
    • doi:10.1046/j.1529-8817.2002.01114.x
    • Guasch H, Paulsson M, Sabater S (2002) Effect of copper on algal communities fromoligotrophic calcareous streams. J Phycol 38:241-248. doi:10.1046/j.1529-8817.2002.01114.x.
    • (2002) J Phycol , vol.38 , pp. 241-248
    • Guasch, H.1    Paulsson, M.2    Sabater, S.3
  • 16
    • 34248393041 scopus 로고    scopus 로고
    • Effect of copper on acid phosphatase activity in yeast Yarrowia lipolytica
    • Ito H, Inouhe M, Tohoyama H, Joho M (2007) Effect of copper on acid phosphatase activity in yeast Yarrowia lipolytica. Z Naturforsch [C] 62:70-76.
    • (2007) Z Naturforsch [C] , vol.62 , pp. 70-76
    • Ito, H.1    Inouhe, M.2    Tohoyama, H.3    Joho, M.4
  • 17
    • 34548775627 scopus 로고    scopus 로고
    • In vitro effect of agriculture pollutants and their joint action on Pseudokirchneriella subcapitata acid phosphatase
    • doi:10.1016/j.chemosphere.2007.06.024
    • Jonsson CM, Aoyama H (2007) In vitro effect of agriculture pollutants and their joint action on Pseudokirchneriella subcapitata acid phosphatase. Chemosphere 69:849-855. doi:10.1016/j.chemosphere.2007.06.024.
    • (2007) Chemosphere , vol.69 , pp. 849-855
    • Jonsson, C.M.1    Aoyama, H.2
  • 19
    • 19544370842 scopus 로고    scopus 로고
    • Risk assessment of the herbicide clomazone in the aquatic life
    • Jonsson CM, Maia AHN, Ferreira CJA et al (1998) Risk assessment of the herbicide clomazone in the aquatic life. Verh Int Verein Limnol 26:1724-1726.
    • (1998) Verh Int Verein Limnol , vol.26 , pp. 1724-1726
    • Jonsson, C.M.1    Maia, A.H.N.2    Ferreira, C.J.A.3
  • 20
    • 0035081389 scopus 로고    scopus 로고
    • Bioconcentration of the insecticide pyridaphenthion by the green algae Chlorella saccharophila
    • doi:10.1016/S0045-6535(00)00145-4
    • Jonsson CM, Paraiba LC, Mendoza MT et al (2001) Bioconcentration of the insecticide pyridaphenthion by the green algae Chlorella saccharophila. Chemosphere 43:321-325. doi:10.1016/S0045-6535(00)00145-4.
    • (2001) Chemosphere , vol.43 , pp. 321-325
    • Jonsson, C.M.1    Paraiba, L.C.2    Mendoza, M.T.3
  • 21
    • 0028977785 scopus 로고
    • Review of wholeorganism bioassay: Soil, freshwater, sediment, and freshwater assessment in Canada
    • doi:10.1006/eesa.1995.1027
    • Keddy CJ, Greene JC, Bonnel MA (1995) Review of wholeorganism bioassay: soil, freshwater, sediment, and freshwater assessment in Canada. Ecotoxicol Environ Saf 30:221-251. doi:10.1006/eesa.1995.1027.
    • (1995) Ecotoxicol Environ Saf , vol.30 , pp. 221-251
    • Keddy, C.J.1    Greene, J.C.2    Bonnel, M.A.3
  • 22
    • 1842477325 scopus 로고    scopus 로고
    • Induction of both acid and alkaline phosphatase activity in two green-algae (Chlorophyceae) in low N and P concentrations
    • doi:10.1023/B:hydr.0000018166. 15764.b0
    • Kruskopf MM, Du Plessis S (2004) Induction of both acid and alkaline phosphatase activity in two green-algae (Chlorophyceae) in low N and P concentrations. Hydrobiologia 513:59-70. doi:10.1023/B:hydr.0000018166. 15764.b0.
    • (2004) Hydrobiologia , vol.513 , pp. 59-70
    • Kruskopf, M.M.1    Du Plessis, S.2
  • 23
    • 0029105269 scopus 로고
    • Effect of combined copper, zinc, chromium and selenium by orthogonal array design on alkaline phosphatase activity in liver of the red sea bream, Chrysophrys major
    • doi:10.1016/0044-8486(94)00326-J
    • Lan WG, Wong MK, Chen N et al (1995) Effect of combined copper, zinc, chromium and selenium by orthogonal array design on alkaline phosphatase activity in liver of the red sea bream, Chrysophrys major. Aquaculture 131:219- 230. doi:10.1016/0044-8486(94)00326-J.
    • (1995) Aquaculture , vol.131 , pp. 219-230
    • Lan, W.G.1    Wong, M.K.2    Chen, N.3
  • 24
    • 0037428333 scopus 로고    scopus 로고
    • Long-term effect of sea-nine on natural coastal phytoplanktonic communities assessed by pollution induced community tolerance
    • doi:10.1016/S0166- 445X(02)00065-6
    • Larsen DK, Wagner I, Gustavson K et al (2003) Long-term effect of sea-nine on natural coastal phytoplanktonic communities assessed by pollution induced community tolerance. Aquat Toxicol 62:35-44. doi:10.1016/S0166- 445X(02)00065-6.
    • (2003) Aquat Toxicol , vol.62 , pp. 35-44
    • Larsen, D.K.1    Wagner, I.2    Gustavson, K.3
  • 25
    • 33751053254 scopus 로고    scopus 로고
    • Effect of copper sulphate treatment on natural phytoplanktonic communities
    • doi:10.1016/j.aquatox.2006.09.004
    • Le Jeune AH, Charpin M, Deluchat V et al (2006) Effect of copper sulphate treatment on natural phytoplanktonic communities. Aquat Toxicol 80:267-280. doi:10.1016/j.aquatox.2006.09.004.
    • (2006) Aquat Toxicol , vol.80 , pp. 267-280
    • Le Jeune, A.H.1    Charpin, M.2    Deluchat, V.3
  • 26
    • 28444442965 scopus 로고    scopus 로고
    • Copper and zinc induction of lipid peroxidation and effects on antioxidant enzyme activities in the microalga Pavlova viridis (Prymnesiophyceae)
    • doi: 10.1016/j.chemosphere.2005.06.029
    • Li M, Hu C, Zhu Q, Chen L et al (2006) Copper and zinc induction of lipid peroxidation and effects on antioxidant enzyme activities in the microalga Pavlova viridis (Prymnesiophyceae). Chemosphere 62:565-572. doi: 10.1016/j.chemosphere.2005.06.029.
    • (2006) Chemosphere , vol.62 , pp. 565-572
    • Li, M.1    Hu, C.2    Zhu, Q.3    Chen, L.4
  • 27
    • 33846393303 scopus 로고    scopus 로고
    • Cytochemical localization of acid phosphatase in Stigeoclonium tenue (Chaetophorales, Chlorophyceae)
    • Michetti KM, Leonardi PI, Cáceres EJ (2006) Cytochemical localization of acid phosphatase in Stigeoclonium tenue (Chaetophorales, Chlorophyceae). Biocell 30:491-496.
    • (2006) Biocell , vol.30 , pp. 491-496
    • Michetti, K.M.1    Leonardi, P.I.2    Cáceres, E.J.3
  • 28
    • 0028219490 scopus 로고
    • Purification and characterization of an acid phosphatase from Mycoplasma fermentans
    • Noda M, Shibata K, Sawa Y et al (1994) Purification and characterization of an acid phosphatase from Mycoplasma fermentans. Microbiol Immunol 38:103-107.
    • (1994) Microbiol Immunol , vol.38 , pp. 103-107
    • Noda, M.1    Shibata, K.2    Sawa, Y.3
  • 30
    • 0036162338 scopus 로고    scopus 로고
    • Algal growth inhibition by river water pollutants in the agricultural area around lake Biwa, Japan
    • doi:10.1016/S0269-7491(01)00196-8
    • Okamura H, Mingyu P, Aoyama I et al (2002) Algal growth inhibition by river water pollutants in the agricultural area around lake Biwa, Japan. Environ Pollut 117:411-419. doi:10.1016/S0269-7491(01)00196-8.
    • (2002) Environ Pollut , vol.117 , pp. 411-419
    • Okamura, H.1    Mingyu, P.2    Aoyama, I.3
  • 31
    • 0016208478 scopus 로고
    • Partial characterization of the intra- and extracellular acid phosphatase of an alga, Ochromonas danica
    • Patni NJ, Aaronson S (1974) Partial characterization of the intra- and extracellular acid phosphatase of an alga, Ochromonas danica. J Gen Microbiol 83:9-20.
    • (1974) J Gen Microbiol , vol.83 , pp. 9-20
    • Patni, N.J.1    Aaronson, S.2
  • 32
    • 0029913795 scopus 로고    scopus 로고
    • New algal enzyme bioassay for the rapid assessment of aquatic toxicity
    • doi:10.1007/s001289900110
    • Peterson SM, Stauber JL (1996) New algal enzyme bioassay for the rapid assessment of aquatic toxicity. Bull Environ Contam Toxicol 56:750-757. doi:10.1007/s001289900110.
    • (1996) Bull Environ Contam Toxicol , vol.56 , pp. 750-757
    • Peterson, S.M.1    Stauber, J.L.2
  • 33
    • 1642567332 scopus 로고    scopus 로고
    • Acid phosphatase activities during the germination of Glycine max seeds
    • doi:10.1016/j.plaphy. 2003.10.009
    • Prazeres JN, Ferreira CV, Aoyama H (2004) Acid phosphatase activities during the germination of Glycine max seeds. Plant Physiol Biochem 42:15-20. doi:10.1016/j.plaphy. 2003.10.009.
    • (2004) Plant Physiol Biochem , vol.42 , pp. 15-20
    • Prazeres, J.N.1    Ferreira, C.V.2    Aoyama, H.3
  • 34
    • 0031413159 scopus 로고    scopus 로고
    • Interactive effects of UV-B and Cu on photosynthesis, uptake and metabolism of nutrients in a green alga Chlorella vulgaris under simulated ozone column
    • doi:10.2323/jgam.43.281
    • Rai PK, Rai LC (1997) Interactive effects of UV-B and Cu on photosynthesis, uptake and metabolism of nutrients in a green alga Chlorella vulgaris under simulated ozone column. J Gen Appl Microbiol 43:281-288. doi:10.2323/jgam.43.281.
    • (1997) J Gen Appl Microbiol , vol.43 , pp. 281-288
    • Rai, P.K.1    Rai, L.C.2
  • 35
    • 0032730441 scopus 로고    scopus 로고
    • Outer membrane lipoprotein e (P4) of Haemophilus influenzae is a novel phosphomonoesterase
    • Reilly TJ, Chance DL, Smith AL (1999) Outer membrane lipoprotein e (P4) of Haemophilus influenzae is a novel phosphomonoesterase. J Bacteriol 181:6797-6805.
    • (1999) J Bacteriol , vol.181 , pp. 6797-6805
    • Reilly, T.J.1    Chance, D.L.2    Smith, A.L.3
  • 36
    • 0011258511 scopus 로고
    • Cytochemical localization of acid phosphatase in Euglena gracilis
    • doi:10.1083/jcb.24.2.235
    • Sommer JR, Blum JJ (1965) Cytochemical localization of acid phosphatase in Euglena gracilis. J Cell Biol 24:235-251. doi:10.1083/jcb.24.2.235.
    • (1965) J Cell Biol , vol.24 , pp. 235-251
    • Sommer, J.R.1    Blum, J.J.2
  • 37
    • 0000940515 scopus 로고
    • Effect of phosphorus limitation on respiratory metabolism in the green algae Selenastrum minutum
    • doi:10.1104/95.4.1089
    • Theodorou ME, Elrifi IR, Turpin DH et al (1991) Effect of phosphorus limitation on respiratory metabolism in the green algae Selenastrum minutum. Plant Physiol 95:1089- 1095. doi:10.1104/pp.95.4.1089.
    • (1991) Plant Physiol , vol.95 , pp. 1089-1095
    • Theodorou, M.E.1    Elrifi, I.R.2    Turpin, D.H.3
  • 38
    • 0015102852 scopus 로고
    • Effects of zinc and other metal ions on the stability and activity of Escherichia coli alkaline phosphatase
    • Trotman NA, Greenwood C (1971) Effects of zinc and other metal ions on the stability and activity of Escherichia coli alkaline phosphatase. Biochem J 124:25-30.
    • (1971) Biochem J , vol.124 , pp. 25-30
    • Trotman, N.A.1    Greenwood, C.2
  • 39
    • 0002536783 scopus 로고
    • Acid phosphatase activity during spore differentiation of the red algae Gigartina teedii and Chondria tenuissima
    • doi: 10.1007/BF00937944
    • Tsekos I, Schnepf E (1991) Acid phosphatase activity during spore differentiation of the red algae Gigartina teedii and Chondria tenuissima. Plant Syst Evol 176:35-51. doi: 10.1007/BF00937944.
    • (1991) Plant Syst Evol , vol.176 , pp. 35-51
    • Tsekos, I.1    Schnepf, E.2
  • 40
    • 0242541596 scopus 로고    scopus 로고
    • Phosphatase production and activity in copper (II) accumulating Rizopus delemar
    • doi:10.1016/j.enzmictec.2003.06.001
    • Tsekova K, Galabova D (2003) Phosphatase production and activity in copper (II) accumulating Rizopus delemar. Enzyme Microb Technol 33:926-931. doi:10.1016/j.enzmictec.2003.06.001.
    • (2003) Enzyme Microb Technol , vol.33 , pp. 926-931
    • Tsekova, K.1    Galabova, D.2
  • 41
    • 0025222988 scopus 로고
    • An enzyme with double identity: Purple acid phosphatase and tartrate-resistant acid phosphatase
    • Vincent JB, Averill BA (1990) An enzyme with double identity: purple acid phosphatase and tartrate-resistant acid phosphatase. FASEB J 4:3009-3013.
    • (1990) FASEB J , vol.4 , pp. 3009-3013
    • Vincent, J.B.1    Averill, B.A.2
  • 42
    • 0029067564 scopus 로고
    • Biotransformation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons and heterocyclic analogs by several green algae and other algal species under gold and white light
    • doi:10.1016/0009-2797 (95)03610-X
    • Warshawsky D, Cody T, Radike M et al (1995) Biotransformation of benzo[a]pyrene and other polycyclic aromatic hydrocarbons and heterocyclic analogs by several green algae and other algal species under gold and white light. Chem Biol Interact 97:131-148. doi:10.1016/0009-2797 (95)03610-X.
    • (1995) Chem Biol Interact , vol.97 , pp. 131-148
    • Warshawsky, D.1    Cody, T.2    Radike, M.3
  • 44
    • 0034098831 scopus 로고    scopus 로고
    • Effects of cadmium on manganese peroxidase. Competitive inhibition of MnII oxidation and thermal stabilization of the enzyme
    • doi:10.1046/j.1432-1327.2000.01173.x
    • Youngs HL, Sundaramoorthy M, Gold MH (2000) Effects of cadmium on manganese peroxidase. Competitive inhibition of MnII oxidation and thermal stabilization of the enzyme. Eur J Biochem 27:1761-1769. doi:10.1046/j.1432- 1327.2000.01173.x.
    • (2000) Eur J Biochem , vol.27 , pp. 1761-1769
    • Youngs, H.L.1    Sundaramoorthy, M.2    Gold, M.H.3


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