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Volumn 109, Issue 6, 2010, Pages 638-644

Spectrophotometric detection of labile zinc(II) released from metallothionein: A simple method to evaluate heavy metal toxicity

Author keywords

Heavy metal toxicity; Labile zinc; Metallothionein; Porphyrin; Vibrio fischeri

Indexed keywords

ABSORPTION CHANGES; BIOLUMINESCENT BACTERIA; CHROMOGENIC REAGENTS; HEAVY METAL TOXICITY; HIGHLY SENSITIVE; INHIBITION ASSAYS; METAL TOXICITY; METALLOTHIONEIN; METALLOTHIONEINS; PORPHYRIN COMPLEXES; SAMPLE SOLUTION; SIMPLE METHOD; SPECTROPHOTOMETRIC DETECTION; SUBMICROMOLAR CONCENTRATIONS; TOXIC METAL IONS; VIBRIO FISCHERI; WATER-SOLUBLE PORPHYRIN;

EID: 77952107231     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2009.11.016     Document Type: Article
Times cited : (10)

References (41)
  • 1
    • 0033840054 scopus 로고    scopus 로고
    • Effects of four inorganic lead compounds on the proliferation and junctional coupling of cultured REL liver cells
    • Apostoli P., Huard C., Chaumontet C., Martel P., Alessio L., and Mazzoleni G. Effects of four inorganic lead compounds on the proliferation and junctional coupling of cultured REL liver cells. Am. J. Ind. Med. 38 (2000) 340-348
    • (2000) Am. J. Ind. Med. , vol.38 , pp. 340-348
    • Apostoli, P.1    Huard, C.2    Chaumontet, C.3    Martel, P.4    Alessio, L.5    Mazzoleni, G.6
  • 3
    • 0029874822 scopus 로고    scopus 로고
    • Assessing the impact of complexation by EDTA and DTPA on heavy metal toxicity using Microtox bioassay
    • Sillanpää M., and Oikari A. Assessing the impact of complexation by EDTA and DTPA on heavy metal toxicity using Microtox bioassay. Chemosphere 32 (1996) 1485-1497
    • (1996) Chemosphere , vol.32 , pp. 1485-1497
    • Sillanpää, M.1    Oikari, A.2
  • 5
    • 0036740112 scopus 로고    scopus 로고
    • Tea catechins protect against lead-induced cytotoxicity, lipid peroxidation, and membrane fluidity in HepG2 cells
    • Chen L., Yang X., Jiao H., and Zhao B. Tea catechins protect against lead-induced cytotoxicity, lipid peroxidation, and membrane fluidity in HepG2 cells. Toxicol. Sci. 69 (2002) 149-156
    • (2002) Toxicol. Sci. , vol.69 , pp. 149-156
    • Chen, L.1    Yang, X.2    Jiao, H.3    Zhao, B.4
  • 6
    • 0030426092 scopus 로고    scopus 로고
    • Evaluation of municipal waste incinerator fly ash toxicity and the role of cadmium by two aquatic toxicity tests
    • Kaneko H. Evaluation of municipal waste incinerator fly ash toxicity and the role of cadmium by two aquatic toxicity tests. Waste Manag. 16 (1996) 555-559
    • (1996) Waste Manag. , vol.16 , pp. 555-559
    • Kaneko, H.1
  • 8
    • 0032791261 scopus 로고    scopus 로고
    • Determination of the heavy metal binding capacity of aquatic samples using MetPLATE: a preliminary study
    • Huang F., Bitton G., and Kong I.C. Determination of the heavy metal binding capacity of aquatic samples using MetPLATE: a preliminary study. Sci. Total Environ. 234 (1999) 139-145
    • (1999) Sci. Total Environ. , vol.234 , pp. 139-145
    • Huang, F.1    Bitton, G.2    Kong, I.C.3
  • 9
    • 37249054563 scopus 로고    scopus 로고
    • Comparative evaluation of the cytotoxicity sensitivity of six fish cell lines to four heavy metals in vitro
    • Tan F., Wang M., Wang W., and Lu Y. Comparative evaluation of the cytotoxicity sensitivity of six fish cell lines to four heavy metals in vitro. Toxicol. In Vitro 22 (2008) 164-170
    • (2008) Toxicol. In Vitro , vol.22 , pp. 164-170
    • Tan, F.1    Wang, M.2    Wang, W.3    Lu, Y.4
  • 10
    • 0019724048 scopus 로고
    • Comparison of three microbial toxicity screening tests with the Microtox test
    • Dutka B.J., and Kwan K.K. Comparison of three microbial toxicity screening tests with the Microtox test. Bull. Environ. Contam. Toxicol. 27 (1981) 753-757
    • (1981) Bull. Environ. Contam. Toxicol. , vol.27 , pp. 753-757
    • Dutka, B.J.1    Kwan, K.K.2
  • 11
    • 19444374324 scopus 로고    scopus 로고
    • Patterns of metals and arsenic poisoning in Vibrio fischeri bacteria
    • Fulladosa E., Murat J.C., Martínez M., and Villaescusa I. Patterns of metals and arsenic poisoning in Vibrio fischeri bacteria. Chemosphere 60 (2005) 43-48
    • (2005) Chemosphere , vol.60 , pp. 43-48
    • Fulladosa, E.1    Murat, J.C.2    Martínez, M.3    Villaescusa, I.4
  • 12
    • 29944445276 scopus 로고    scopus 로고
    • A review on advantages of implementing luminescence inhibition test (Vibrio fischeri) for acute toxicity prediction of chemicals
    • Parvez S., Venkataraman C., and Mukherji S. A review on advantages of implementing luminescence inhibition test (Vibrio fischeri) for acute toxicity prediction of chemicals. Environ. Int. 32 (2006) 265-268
    • (2006) Environ. Int. , vol.32 , pp. 265-268
    • Parvez, S.1    Venkataraman, C.2    Mukherji, S.3
  • 13
    • 0017870541 scopus 로고
    • Enzyme thermistor analysis of heavy metal ions with use of immobilized urease
    • Mattiasson B., Danielsson B., Hermansson C., and Mosbach K. Enzyme thermistor analysis of heavy metal ions with use of immobilized urease. FEBS Lett. 85 (1978) 203-206
    • (1978) FEBS Lett. , vol.85 , pp. 203-206
    • Mattiasson, B.1    Danielsson, B.2    Hermansson, C.3    Mosbach, K.4
  • 14
    • 0027439347 scopus 로고
    • Lead-protein interactions as a basis for lead toxicity
    • Goering P.L. Lead-protein interactions as a basis for lead toxicity. Neurotoxicology 14 (1993) 45-60
    • (1993) Neurotoxicology , vol.14 , pp. 45-60
    • Goering, P.L.1
  • 17
    • 33645517842 scopus 로고    scopus 로고
    • Biosynthetic regulation of phytochelatins, heavy metal-binding peptides
    • Hirata K., Tsuji N., and Miyamoto K. Biosynthetic regulation of phytochelatins, heavy metal-binding peptides. J. Biosci. Bioeng. 100 (2005) 593-599
    • (2005) J. Biosci. Bioeng. , vol.100 , pp. 593-599
    • Hirata, K.1    Tsuji, N.2    Miyamoto, K.3
  • 19
    • 0002106617 scopus 로고
    • Evolution, structure and chemical activities of class 1 metallothioneins: An overview
    • Suzuki K.T., Imura N., and Kimura M. (Eds), Birkhäuser Verlag, Basel
    • Kagi J.H.R. Evolution, structure and chemical activities of class 1 metallothioneins: An overview. In: Suzuki K.T., Imura N., and Kimura M. (Eds). Metallothionein III (1993), Birkhäuser Verlag, Basel 29-55
    • (1993) Metallothionein III , pp. 29-55
    • Kagi, J.H.R.1
  • 20
    • 0015899751 scopus 로고
    • Evaluation of metallothionein content in animal tissues
    • Piotrowski J.K., Bolanowska W., and Sapota A. Evaluation of metallothionein content in animal tissues. Acta Biochim. Pol. 20 (1973) 207-215
    • (1973) Acta Biochim. Pol. , vol.20 , pp. 207-215
    • Piotrowski, J.K.1    Bolanowska, W.2    Sapota, A.3
  • 21
    • 0018745152 scopus 로고
    • Effect of cadmium, mercury, and bismuth on the copper content in rat tissues
    • Szymańska J.A., and Zelazowski A.J. Effect of cadmium, mercury, and bismuth on the copper content in rat tissues. Environ. Res. 19 (1979) 121-126
    • (1979) Environ. Res. , vol.19 , pp. 121-126
    • Szymańska, J.A.1    Zelazowski, A.J.2
  • 22
    • 0028125990 scopus 로고
    • Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-1
    • Palmiter R.D. Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-1. Proc. Natl. Acad. Sci. USA 91 (1994) 1219-1223
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1219-1223
    • Palmiter, R.D.1
  • 23
    • 0035205337 scopus 로고    scopus 로고
    • Molecular mechanism of the metallothionein gene expression mediated by metal-responsive transcription factor 1
    • Otsuka F. Molecular mechanism of the metallothionein gene expression mediated by metal-responsive transcription factor 1. J. Health Sci. 47 (2001) 513-519
    • (2001) J. Health Sci. , vol.47 , pp. 513-519
    • Otsuka, F.1
  • 24
    • 0037100631 scopus 로고    scopus 로고
    • Mammalian metal response element-binding transcription factor-1 functions as a zinc sensor in yeast, but not as a sensor of cadmium or oxidative stress
    • Daniels P.J., Bittel D., Smirnova I.V., Winge D.R., and Andrews G.K. Mammalian metal response element-binding transcription factor-1 functions as a zinc sensor in yeast, but not as a sensor of cadmium or oxidative stress. Nucleic Acids Res. 30 (2002) 3130-3140
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3130-3140
    • Daniels, P.J.1    Bittel, D.2    Smirnova, I.V.3    Winge, D.R.4    Andrews, G.K.5
  • 25
    • 34047217992 scopus 로고    scopus 로고
    • Mechanism of metallothionein gene activation mediated by heavy-metal dependent transcription factor MTF-1
    • (in Japanese)
    • Otsuka F., Ohno S., Suzuki K., Takahashi K., Ohsawa M., and Koizumi S. Mechanism of metallothionein gene activation mediated by heavy-metal dependent transcription factor MTF-1. Yakugaku Zasshi 127 (2007) 675-684 (in Japanese)
    • (2007) Yakugaku Zasshi , vol.127 , pp. 675-684
    • Otsuka, F.1    Ohno, S.2    Suzuki, K.3    Takahashi, K.4    Ohsawa, M.5    Koizumi, S.6
  • 26
    • 84996018252 scopus 로고
    • Spectrophotometric and analogue derivative spectrophotometric determination of trace zinc with 5,10,15,20-tetrakis(4-sulfophenyl)porphine in presence of high concentrations of cadmium
    • Ishii H., and Tsuchiai H. Spectrophotometric and analogue derivative spectrophotometric determination of trace zinc with 5,10,15,20-tetrakis(4-sulfophenyl)porphine in presence of high concentrations of cadmium. Anal. Sci. 3 (1987) 229-233
    • (1987) Anal. Sci. , vol.3 , pp. 229-233
    • Ishii, H.1    Tsuchiai, H.2
  • 27
    • 0027359185 scopus 로고
    • Spectrofluorimetric determination of traces of zinc with the cadmium-α,β,γ,δ-tetrakis(4-sulphophenyl)-porphine complex
    • Igarashi S., and Yotsuyanagi T. Spectrofluorimetric determination of traces of zinc with the cadmium-α,β,γ,δ-tetrakis(4-sulphophenyl)-porphine complex. Anal. Chim. Acta 281 (1993) 347-351
    • (1993) Anal. Chim. Acta , vol.281 , pp. 347-351
    • Igarashi, S.1    Yotsuyanagi, T.2
  • 28
    • 0002371107 scopus 로고    scopus 로고
    • Equilibria, kinetics and mechanism of complexation of 5,10,15,20-tetrakis(4-sulfonatophenyl)porphyrin and its N-methylated derivative with cadmium(II) and zinc(II) ions in aqueous solution at various temperatures and pressures. Effects of metal ion size and porphyrin ring deformation on metal ion incorporation
    • Inamo M., Tomita A., Inagaki Y., Asano N., Suenaga K., Tabata M., and Funahashi S. Equilibria, kinetics and mechanism of complexation of 5,10,15,20-tetrakis(4-sulfonatophenyl)porphyrin and its N-methylated derivative with cadmium(II) and zinc(II) ions in aqueous solution at various temperatures and pressures. Effects of metal ion size and porphyrin ring deformation on metal ion incorporation. Inorg. Chim. 256 (1997) 77-85
    • (1997) Inorg. Chim. , vol.256 , pp. 77-85
    • Inamo, M.1    Tomita, A.2    Inagaki, Y.3    Asano, N.4    Suenaga, K.5    Tabata, M.6    Funahashi, S.7
  • 29
    • 0021829810 scopus 로고
    • Distinct metal-binding configurations in metallothionein
    • Nielson K.B., Atkin C.L., and Winge D.R. Distinct metal-binding configurations in metallothionein. J. Biol. Chem. 260 (1985) 5342-5350
    • (1985) J. Biol. Chem. , vol.260 , pp. 5342-5350
    • Nielson, K.B.1    Atkin, C.L.2    Winge, D.R.3
  • 30
    • 33846893875 scopus 로고    scopus 로고
    • Bismuth-norfloxacin complex: Synthesis, physicochemical and antimicrobial evaluation
    • Shaikh A.R., Giridhar R., and Yadav M.R. Bismuth-norfloxacin complex: Synthesis, physicochemical and antimicrobial evaluation. Int. J. Pharm. 332 (2007) 24-30
    • (2007) Int. J. Pharm. , vol.332 , pp. 24-30
    • Shaikh, A.R.1    Giridhar, R.2    Yadav, M.R.3
  • 31
    • 7444238111 scopus 로고    scopus 로고
    • Immobilization of metallothionein as a sensitive biosensor chip for the detection of metal ions by surface plasmon resonance
    • Wu C.M., and Lin L.Y. Immobilization of metallothionein as a sensitive biosensor chip for the detection of metal ions by surface plasmon resonance. Biosens. Bioelectron. 20 (2004) 864-871
    • (2004) Biosens. Bioelectron. , vol.20 , pp. 864-871
    • Wu, C.M.1    Lin, L.Y.2
  • 32
    • 33745796028 scopus 로고    scopus 로고
    • Construction of an additional metal-binding site in human metallothionein-2
    • Toyama M., Sasaki M., Hirayama N., Murooka Y., and Yamashita M. Construction of an additional metal-binding site in human metallothionein-2. J. Biosci. Bioeng. 101 (2006) 354-360
    • (2006) J. Biosci. Bioeng. , vol.101 , pp. 354-360
    • Toyama, M.1    Sasaki, M.2    Hirayama, N.3    Murooka, Y.4    Yamashita, M.5
  • 34
    • 0016198697 scopus 로고
    • Conversion of metallothionein into Cu-thionein, the possible low molecular weight form of neonatal hepatic mitochondrocuprein
    • Rupp H., and Weser U. Conversion of metallothionein into Cu-thionein, the possible low molecular weight form of neonatal hepatic mitochondrocuprein. FEBS Lett. 44 (1974) 293-297
    • (1974) FEBS Lett. , vol.44 , pp. 293-297
    • Rupp, H.1    Weser, U.2
  • 35
    • 0016720649 scopus 로고
    • Copper-chelatin: Purification and properties of a copper-binding protein from rat liver
    • Winge D.R., Premakumar R., Wiley R.D., and Rajagopalan K.V. Copper-chelatin: Purification and properties of a copper-binding protein from rat liver. Arch. Biochem. Biophys. 170 (1975) 253-266
    • (1975) Arch. Biochem. Biophys. , vol.170 , pp. 253-266
    • Winge, D.R.1    Premakumar, R.2    Wiley, R.D.3    Rajagopalan, K.V.4
  • 36
    • 0020006959 scopus 로고
    • Metal binding sites of rat liver Cu-thionein
    • Geller B.L., and Winge D.R. Metal binding sites of rat liver Cu-thionein. Arch. Biochem. Biophys. 213 (1982) 109-117
    • (1982) Arch. Biochem. Biophys. , vol.213 , pp. 109-117
    • Geller, B.L.1    Winge, D.R.2
  • 37
    • 11144273171 scopus 로고    scopus 로고
    • Study on the toxicity of binary equitoxic mixtures of metals using the luminescent bacteria Vibrio fischeri as a biological target
    • Fulladosa E., Murat J.C., and Villaescusa I. Study on the toxicity of binary equitoxic mixtures of metals using the luminescent bacteria Vibrio fischeri as a biological target. Chemosphere 58 (2005) 551-557
    • (2005) Chemosphere , vol.58 , pp. 551-557
    • Fulladosa, E.1    Murat, J.C.2    Villaescusa, I.3
  • 38
    • 33747765607 scopus 로고    scopus 로고
    • Cr(VI) reduction into Cr(III) as a mechanism to explain the low sensitivity of Vibrio fischeri bioassay to detect chromium pollution
    • Fulladosa E., Desjardin V., Murat J.C., Gourdon R., and Villaescusa I. Cr(VI) reduction into Cr(III) as a mechanism to explain the low sensitivity of Vibrio fischeri bioassay to detect chromium pollution. Chemosphere 65 (2006) 644-650
    • (2006) Chemosphere , vol.65 , pp. 644-650
    • Fulladosa, E.1    Desjardin, V.2    Murat, J.C.3    Gourdon, R.4    Villaescusa, I.5
  • 40
    • 0342426681 scopus 로고    scopus 로고
    • The use of luminescent bacteria for measuring chronic toxicity
    • Ostrander G.K. (Ed), CRC, Boca Raton
    • Bulich A.A., Huynh H., and Ulitzur S. The use of luminescent bacteria for measuring chronic toxicity. In: Ostrander G.K. (Ed). Techniques in aquatic toxicology vol. 2 (1996), CRC, Boca Raton 3-12
    • (1996) Techniques in aquatic toxicology , vol.2 , pp. 3-12
    • Bulich, A.A.1    Huynh, H.2    Ulitzur, S.3
  • 41
    • 0033199073 scopus 로고    scopus 로고
    • Rapid method for detection and detoxification of heavy metal ions in water environments using phytochelation
    • Satofuka H., Amano S., Atomi H., Takagi M., Hirata K., Miyamoto K., and Imanaka T. Rapid method for detection and detoxification of heavy metal ions in water environments using phytochelation. J. Biosci. Bioeng. 88 (1999) 287-292
    • (1999) J. Biosci. Bioeng. , vol.88 , pp. 287-292
    • Satofuka, H.1    Amano, S.2    Atomi, H.3    Takagi, M.4    Hirata, K.5    Miyamoto, K.6    Imanaka, T.7


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