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Volumn 144, Issue 2, 2006, Pages 122-129

Identification, sequencing and expression of selenium-dependent glutathione peroxidase transcript in the freshwater bivalve Unio tumidus exposed to Aroclor 1254

Author keywords

Aroclor; Coding sequence; Expression level; Freshwater bivalve; Pi GST; RACE PCR; RT PCR; Se GPx; Unio tumidus

Indexed keywords

AMINO ACID; AROCLOR 1254; COMPLEMENTARY DNA; FRESH WATER; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; MESSENGER RNA; PRIMER DNA; PROTEIN; SELENIUM; SELENOCYSTEINE;

EID: 33750159082     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2006.07.002     Document Type: Article
Times cited : (30)

References (54)
  • 1
    • 0031733938 scopus 로고    scopus 로고
    • Liver glutathione content and glutathione-dependent enzymes of two species of freshwater fishes as bioindicators of chemical pollution
    • Almar M., Otero L., Santos C., and Gallegho J.G. Liver glutathione content and glutathione-dependent enzymes of two species of freshwater fishes as bioindicators of chemical pollution. J. Environ. Sci. Health 33 (1998) 769-783
    • (1998) J. Environ. Sci. Health , vol.33 , pp. 769-783
    • Almar, M.1    Otero, L.2    Santos, C.3    Gallegho, J.G.4
  • 3
    • 0034489653 scopus 로고    scopus 로고
    • The glutathione peroxidases
    • Arthur J.R. The glutathione peroxidases. Cell. Mol. Life Sci. 57 (2000) 1825-1835
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1825-1835
    • Arthur, J.R.1
  • 4
    • 0031227819 scopus 로고    scopus 로고
    • Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling
    • Aumann K.D., Bedorf N., Brigelius-Flohé R., Schomburg D., and Flohé L. Glutathione peroxidase revisited-simulation of the catalytic cycle by computer-assisted molecular modelling. Biomed. Environ. Sci. 10 (1997) 136-155
    • (1997) Biomed. Environ. Sci. , vol.10 , pp. 136-155
    • Aumann, K.D.1    Bedorf, N.2    Brigelius-Flohé, R.3    Schomburg, D.4    Flohé, L.5
  • 5
    • 52649160725 scopus 로고    scopus 로고
    • Induction of glutathione S-transferase in the northern quahog Mercenaria mercenaria after exposure to the polychlorinated biphenyl (PCB) mixture Aroclor 1248
    • Blanchette B.N., and Singh B.R. Induction of glutathione S-transferase in the northern quahog Mercenaria mercenaria after exposure to the polychlorinated biphenyl (PCB) mixture Aroclor 1248. J. Protein Chem. 21 (2002) 489-494
    • (2002) J. Protein Chem. , vol.21 , pp. 489-494
    • Blanchette, B.N.1    Singh, B.R.2
  • 6
    • 0023891262 scopus 로고
    • Elevation of glutathione S-transferase activity as a stress response to organochlorine compounds, in the freshwater mussel, Sphaerium corneum
    • Boryslawsky M., Garood A.C., and Pearson J.T. Elevation of glutathione S-transferase activity as a stress response to organochlorine compounds, in the freshwater mussel, Sphaerium corneum. Mar. Environ. Res. 24 (1988) 101-104
    • (1988) Mar. Environ. Res. , vol.24 , pp. 101-104
    • Boryslawsky, M.1    Garood, A.C.2    Pearson, J.T.3
  • 8
    • 7744226001 scopus 로고    scopus 로고
    • Total oxyradical scavenging capacity responses in Mytilus galloprovincialis transplanted into the Venice lagoon (Italy) to measure the biological impact of anthropogenic activities
    • Camus L., Pampanin D.M., Volpato E., Delaney E., Sanni S., and Nasci C. Total oxyradical scavenging capacity responses in Mytilus galloprovincialis transplanted into the Venice lagoon (Italy) to measure the biological impact of anthropogenic activities. Mar. Pollut. Bull. 49 (2004) 801-808
    • (2004) Mar. Pollut. Bull. , vol.49 , pp. 801-808
    • Camus, L.1    Pampanin, D.M.2    Volpato, E.3    Delaney, E.4    Sanni, S.5    Nasci, C.6
  • 9
    • 0022730806 scopus 로고
    • The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon TGA
    • Chambers I., Frampton J., Goldfarb P., Affara N., Mcbain W., and Harrison P. The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon TGA. EMBO J. 5 (1986) 1221-1227
    • (1986) EMBO J. , vol.5 , pp. 1221-1227
    • Chambers, I.1    Frampton, J.2    Goldfarb, P.3    Affara, N.4    Mcbain, W.5    Harrison, P.6
  • 10
    • 2942744630 scopus 로고    scopus 로고
    • A comparative study of the expression of CYP1A and CYP4 genes in aquatic invertebrate (freshwater mussel, Unio tumidus) and vertebrate (rainbow trout, Oncorhynchus mykiss)
    • Chaty S., Rodius F., and Vasseur P. A comparative study of the expression of CYP1A and CYP4 genes in aquatic invertebrate (freshwater mussel, Unio tumidus) and vertebrate (rainbow trout, Oncorhynchus mykiss). Aquat. Toxicol. 69 (2004) 81-93
    • (2004) Aquat. Toxicol. , vol.69 , pp. 81-93
    • Chaty, S.1    Rodius, F.2    Vasseur, P.3
  • 11
    • 0027536023 scopus 로고
    • Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI
    • Chu F.F., Doroshow J.H., and Esworhty R.S. Expression, characterization, and tissue distribution of a new cellular selenium-dependent glutathione peroxidase, GSHPx-GI. J. Biol. Chem. 268 (1993) 2571-2576
    • (1993) J. Biol. Chem. , vol.268 , pp. 2571-2576
    • Chu, F.F.1    Doroshow, J.H.2    Esworhty, R.S.3
  • 12
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16 (1988) 10881-10890
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 13
    • 0031280403 scopus 로고    scopus 로고
    • Glutathione reductase, selenium-dependent glutathione peroxidase, glutathione levels, and lipid peroxidation in freshwater bivalves, Unio tumidus, as biomarkers of aquatic contamination in field studies
    • Cossu C., Doyotte A., Jacquin M.C., Babut M., Exinger A., and Vasseur P. Glutathione reductase, selenium-dependent glutathione peroxidase, glutathione levels, and lipid peroxidation in freshwater bivalves, Unio tumidus, as biomarkers of aquatic contamination in field studies. Ecotoxicol. Environ. Saf. 38 (1997) 122-131
    • (1997) Ecotoxicol. Environ. Saf. , vol.38 , pp. 122-131
    • Cossu, C.1    Doyotte, A.2    Jacquin, M.C.3    Babut, M.4    Exinger, A.5    Vasseur, P.6
  • 14
    • 0033950088 scopus 로고    scopus 로고
    • Antioxidant biomarkers in freshwater bivalves, Unio tumidus, in response to different contamination profiles of aquatic sediments
    • Cossu C., Doyotte A., Babut M., Exinger A., and Vasseur P. Antioxidant biomarkers in freshwater bivalves, Unio tumidus, in response to different contamination profiles of aquatic sediments. Ecotoxicol. Environ. Saf. 45 (2000) 106-121
    • (2000) Ecotoxicol. Environ. Saf. , vol.45 , pp. 106-121
    • Cossu, C.1    Doyotte, A.2    Babut, M.3    Exinger, A.4    Vasseur, P.5
  • 15
    • 20444390679 scopus 로고    scopus 로고
    • cDNA cloning and expression pattern of pi-class glutathione S-transferase in the freshwater bivalves Unio tumidus and Corbicula fluminea
    • Doyen P., Vasseur P., and Rodius F. cDNA cloning and expression pattern of pi-class glutathione S-transferase in the freshwater bivalves Unio tumidus and Corbicula fluminea. Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. 140 (2005) 300-308
    • (2005) Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. , vol.140 , pp. 300-308
    • Doyen, P.1    Vasseur, P.2    Rodius, F.3
  • 16
    • 0030824222 scopus 로고    scopus 로고
    • Antioxidant enzymes, glutathione and lipid peroxidation as relevant biomarkers of experimental or field exposure in the gills and in the digestive gland of the freshwater bivalve Unio tumidus
    • Doyotte A., Cossu C., Jacquin M.-C., Babut M., and Vasseur P. Antioxidant enzymes, glutathione and lipid peroxidation as relevant biomarkers of experimental or field exposure in the gills and in the digestive gland of the freshwater bivalve Unio tumidus. Aquat. Toxicol. 39 (1997) 93-110
    • (1997) Aquat. Toxicol. , vol.39 , pp. 93-110
    • Doyotte, A.1    Cossu, C.2    Jacquin, M.-C.3    Babut, M.4    Vasseur, P.5
  • 17
    • 0031879339 scopus 로고    scopus 로고
    • Selenium dependent glutathione-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine
    • Esworthy R.S., Swiderek K.M., Ho Y.S., and Chu F.F. Selenium dependent glutathione-GI is a major glutathione peroxidase activity in the mucosal epithelium of rodent intestine. Biochim. Biophys. Acta 1381 (1998) 213-226
    • (1998) Biochim. Biophys. Acta , vol.1381 , pp. 213-226
    • Esworthy, R.S.1    Swiderek, K.M.2    Ho, Y.S.3    Chu, F.F.4
  • 18
    • 0015880169 scopus 로고
    • Glutathione peroxidase: a selenoenzyme
    • Flohé L., Gunzler W.A., and Schock H.H. Glutathione peroxidase: a selenoenzyme. FEBS Lett. 32 (1973) 132-134
    • (1973) FEBS Lett. , vol.32 , pp. 132-134
    • Flohé, L.1    Gunzler, W.A.2    Schock, H.H.3
  • 19
    • 0017889205 scopus 로고
    • Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine
    • Forstrom J.W., Zakowski J.J., and Tappel A.L. Identification of the catalytic site of rat liver glutathione peroxidase as selenocysteine. Biochemistry 17 (1978) 2639-2644
    • (1978) Biochemistry , vol.17 , pp. 2639-2644
    • Forstrom, J.W.1    Zakowski, J.J.2    Tappel, A.L.3
  • 20
    • 0345982213 scopus 로고    scopus 로고
    • Complete PCB congener distributions for 17 Aroclor mixtures determined by 3 HRGC systems optimized for comprehensive, quantitative, congener-specific analysis
    • Frame G.M., Cochran J.W., and Boewadt S.S. Complete PCB congener distributions for 17 Aroclor mixtures determined by 3 HRGC systems optimized for comprehensive, quantitative, congener-specific analysis. J. High Resolut. Chromatogr. 19 (1996) 657-668
    • (1996) J. High Resolut. Chromatogr. , vol.19 , pp. 657-668
    • Frame, G.M.1    Cochran, J.W.2    Boewadt, S.S.3
  • 22
    • 0025602326 scopus 로고
    • A mouse cDNA sequence for epididymal androgen-regulated proteins related to glutathione peroxidase
    • Ghyselinck N.B., and Dufaure J.P. A mouse cDNA sequence for epididymal androgen-regulated proteins related to glutathione peroxidase. Nucleic Acids Res. 18 (1990) 7144-7144
    • (1990) Nucleic Acids Res. , vol.18 , pp. 7144-7144
    • Ghyselinck, N.B.1    Dufaure, J.P.2
  • 24
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes J.D., and Pulford D.J. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30 (1995) 445-600
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 25
    • 0002486606 scopus 로고
    • Nucleotide sequence of a rat glutathione peroxidase
    • Ho Y.-S., Howard A.J., and Crapo J.D. Nucleotide sequence of a rat glutathione peroxidase. Nucleic Acids Res. 16 (1988) 5207
    • (1988) Nucleic Acids Res. , vol.16 , pp. 5207
    • Ho, Y.-S.1    Howard, A.J.2    Crapo, J.D.3
  • 26
    • 0343182989 scopus 로고    scopus 로고
    • Effects of non-ortho-substituted polychlorinated biphenyls (congeners 77 and 126) on cytochrome P4501A and conjugation activites in rainbow trout (Oncorhynchus mykiss)
    • Huuskonen S., Lindstrom-Seppa P., Koponen K., and Roy S. Effects of non-ortho-substituted polychlorinated biphenyls (congeners 77 and 126) on cytochrome P4501A and conjugation activites in rainbow trout (Oncorhynchus mykiss). Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. 113 (1996) 205-213
    • (1996) Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. , vol.113 , pp. 205-213
    • Huuskonen, S.1    Lindstrom-Seppa, P.2    Koponen, K.3    Roy, S.4
  • 29
    • 0032427819 scopus 로고    scopus 로고
    • Congener-specific distribution of polychlorinated biphenyls in brain regions, blood, liver and fat of adult rats following repeated exposure to Aroclor 1254
    • Kodavanti P.R., Ward T.R., Derr-Yellin E.C., Mundy W.R., Casey A.C., Bush B., and Tilson H.A. Congener-specific distribution of polychlorinated biphenyls in brain regions, blood, liver and fat of adult rats following repeated exposure to Aroclor 1254. Toxicol. Appl. Pharmacol. 153 (1998) 199-210
    • (1998) Toxicol. Appl. Pharmacol. , vol.153 , pp. 199-210
    • Kodavanti, P.R.1    Ward, T.R.2    Derr-Yellin, E.C.3    Mundy, W.R.4    Casey, A.C.5    Bush, B.6    Tilson, H.A.7
  • 30
    • 0022885217 scopus 로고
    • Glutathione peroxidase on approval
    • Bannister J.V., and Michelson A.M. (Eds)
    • Ladenstein R., Epp O., Gunzler W.A., and Flohé L. Glutathione peroxidase on approval. In: Bannister J.V., and Michelson A.M. (Eds). In Life Chemistry Reports 14 (1986) 37-55
    • (1986) In Life Chemistry Reports , vol.14 , pp. 37-55
    • Ladenstein, R.1    Epp, O.2    Gunzler, W.A.3    Flohé, L.4
  • 31
    • 0024269217 scopus 로고
    • Glutathione transferases-structure and catalytic activity
    • Mannervik B., and Danielson U.H. Glutathione transferases-structure and catalytic activity. Crit. Rev. Biochem. 23 (1988) 283-337
    • (1988) Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 33
    • 70449174079 scopus 로고
    • Hemoglobin catabolism: I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown
    • Mills G.C. Hemoglobin catabolism: I. Glutathione peroxidase, an erythrocyte enzyme which protects hemoglobin from oxidative breakdown. J. Biol. Chem. 229 (1957) 189-197
    • (1957) J. Biol. Chem. , vol.229 , pp. 189-197
    • Mills, G.C.1
  • 34
    • 0023649866 scopus 로고
    • Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine
    • Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., and Hallewell R.A. Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine. Nucleic Acids Res. 15 (1987) 5854
    • (1987) Nucleic Acids Res. , vol.15 , pp. 5854
    • Mullenbach, G.T.1    Tabrizi, A.2    Irvine, B.D.3    Bell, G.I.4    Hallewell, R.A.5
  • 35
    • 0030002618 scopus 로고    scopus 로고
    • Mixed-function oxidase enzyme activity and oxidative stress in lake trout (Salvelinus namaycush) exposed to 3,3′,4,4′,5-pentachlorobiphenyl (PCB-126)
    • Palace V.P., Klaverkamp J.F., Lockhart W.L., Metnet D.A., Muir D.C.G., and Brown S.B. Mixed-function oxidase enzyme activity and oxidative stress in lake trout (Salvelinus namaycush) exposed to 3,3′,4,4′,5-pentachlorobiphenyl (PCB-126). Environ. Toxicol. Chem. 15 (1996) 955-960
    • (1996) Environ. Toxicol. Chem. , vol.15 , pp. 955-960
    • Palace, V.P.1    Klaverkamp, J.F.2    Lockhart, W.L.3    Metnet, D.A.4    Muir, D.C.G.5    Brown, S.B.6
  • 36
    • 0037038087 scopus 로고    scopus 로고
    • Induction of cytosolic glutathione S-transferases from Atlantic eel (Anguilla anguilla) after intraperitoneal treatment with polychlorinated biphenyls
    • Perez-Lopez M., Valinas M.C.N., and Riol M.J. Induction of cytosolic glutathione S-transferases from Atlantic eel (Anguilla anguilla) after intraperitoneal treatment with polychlorinated biphenyls. Sci. Total Environ. 297 (2002) 141-151
    • (2002) Sci. Total Environ. , vol.297 , pp. 141-151
    • Perez-Lopez, M.1    Valinas, M.C.N.2    Riol, M.J.3
  • 37
    • 0037114448 scopus 로고    scopus 로고
    • Glutathione S-transferase cytosolic isoforms as biomarkers of polychlorinated biphenyl (Arochlor-1254) experimental contamination in rainbow trout
    • Perez-Lopez M., Valinas M.C.N., and Riol M.J. Glutathione S-transferase cytosolic isoforms as biomarkers of polychlorinated biphenyl (Arochlor-1254) experimental contamination in rainbow trout. Toxicol. Lett. 136 (2002) 97-106
    • (2002) Toxicol. Lett. , vol.136 , pp. 97-106
    • Perez-Lopez, M.1    Valinas, M.C.N.2    Riol, M.J.3
  • 38
    • 1842410124 scopus 로고    scopus 로고
    • Glutathione-dependent detoxifying enzymes in rainbow trout liver: search for specific biochemical markers of chemical stress
    • Petrivalsky M., Machala M., Nezveda K., Piacka V., Svobodova Z., and Drabek P. Glutathione-dependent detoxifying enzymes in rainbow trout liver: search for specific biochemical markers of chemical stress. Environ. Toxicol. Chem. 16 (1997) 1417-1421
    • (1997) Environ. Toxicol. Chem. , vol.16 , pp. 1417-1421
    • Petrivalsky, M.1    Machala, M.2    Nezveda, K.3    Piacka, V.4    Svobodova, Z.5    Drabek, P.6
  • 39
    • 0037073278 scopus 로고    scopus 로고
    • Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments
    • Petushok N., Gabryelak T., Palecz D., Zavodnik L., Varga I.S., and Deer K.A. Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments. Aquat. Toxicol. 61 (2002) 65-72
    • (2002) Aquat. Toxicol. , vol.61 , pp. 65-72
    • Petushok, N.1    Gabryelak, T.2    Palecz, D.3    Zavodnik, L.4    Varga, I.S.5    Deer, K.A.6
  • 40
    • 0031047979 scopus 로고    scopus 로고
    • Cloning and localization of a glutathione S-transferase class I gene from Anopheles gambiae
    • Ranson H., Cornel A.J., Fournier D., Vaughan A., Collins F., and Hemingway J. Cloning and localization of a glutathione S-transferase class I gene from Anopheles gambiae. J. Biol.Chem. 272 (1997) 5464-5468
    • (1997) J. Biol.Chem. , vol.272 , pp. 5464-5468
    • Ranson, H.1    Cornel, A.J.2    Fournier, D.3    Vaughan, A.4    Collins, F.5    Hemingway, J.6
  • 41
    • 0037674821 scopus 로고    scopus 로고
    • The role of abiotic factors and pesticide levels on enzymatic activity in the freshwater mussel Anodonta cygnea at three different exposure sites
    • Robillard S., Beauchamp G., and Laulier M. The role of abiotic factors and pesticide levels on enzymatic activity in the freshwater mussel Anodonta cygnea at three different exposure sites. Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. 135 (2003) 49-59
    • (2003) Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. , vol.135 , pp. 49-59
    • Robillard, S.1    Beauchamp, G.2    Laulier, M.3
  • 42
    • 0037382197 scopus 로고    scopus 로고
    • Mussel transplantation and biomarkers as useful tools for assessing water quality in the NW Mediterranean
    • Romeo M., Hoarau P., Garello G., Gnassia-Barelli M., and Girard J.-P. Mussel transplantation and biomarkers as useful tools for assessing water quality in the NW Mediterranean. Environ. Pollut. 122 (2003) 369-378
    • (2003) Environ. Pollut. , vol.122 , pp. 369-378
    • Romeo, M.1    Hoarau, P.2    Garello, G.3    Gnassia-Barelli, M.4    Girard, J.-P.5
  • 44
    • 0032955185 scopus 로고    scopus 로고
    • Glutathione S-transferases, a review
    • Salinas A.E., and Wong M.G. Glutathione S-transferases, a review. Curr. Med. Chem. 6 (1999) 279-309
    • (1999) Curr. Med. Chem. , vol.6 , pp. 279-309
    • Salinas, A.E.1    Wong, M.G.2
  • 45
    • 0035890484 scopus 로고    scopus 로고
    • Structure, function and evolution of glutathione S-transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily
    • Sheehan D., Meade G., Foley V.M., and Dowd C. Structure, function and evolution of glutathione S-transferases: implications for classification of non-mammalian members of an ancient enzyme superfamily. Biochem. J. 360 (2001) 1-16
    • (2001) Biochem. J. , vol.360 , pp. 1-16
    • Sheehan, D.1    Meade, G.2    Foley, V.M.3    Dowd, C.4
  • 46
    • 0022179464 scopus 로고
    • Differential regulation of hepatic glutathione transferase and glutathione peroxidase activities in the rat
    • Schramm H., Roberston L.W., and Oesch F. Differential regulation of hepatic glutathione transferase and glutathione peroxidase activities in the rat. Biochem. Pharmacol. 34 (1985) 3735-3739
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3735-3739
    • Schramm, H.1    Roberston, L.W.2    Oesch, F.3
  • 48
    • 0023186348 scopus 로고
    • Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme
    • Takahashi K., Avissar N., Whitin J., and Cohen H. Purification and characterization of human plasma glutathione peroxidase: a selenoglycoprotein distinct from the known cellular enzyme. Arch. Biochem. Biophys. 256 (1987) 677-686
    • (1987) Arch. Biochem. Biophys. , vol.256 , pp. 677-686
    • Takahashi, K.1    Avissar, N.2    Whitin, J.3    Cohen, H.4
  • 49
    • 0020065662 scopus 로고
    • Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides
    • Ursini F., Maiorino M., Valente M., Ferri L., and Gregolin C. Purification from pig liver of a protein which protects liposomes and biomembranes from peroxidative degradation and exhibits glutathione peroxidase activity on phosphatidylcholine hydroperoxides. Biochim. Biophys. Acta 710 (1982) 197-211
    • (1982) Biochim. Biophys. Acta , vol.710 , pp. 197-211
    • Ursini, F.1    Maiorino, M.2    Valente, M.3    Ferri, L.4    Gregolin, C.5
  • 52
    • 0035126550 scopus 로고    scopus 로고
    • Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea
    • Vidal M.-L., Bassères A., and Narbonne J.-F. Potential biomarkers of trichloroethylene and toluene exposure in Corbicula fluminea. Environ. Toxicol. Pharmacol. 9 (2001) 87-97
    • (2001) Environ. Toxicol. Pharmacol. , vol.9 , pp. 87-97
    • Vidal, M.-L.1    Bassères, A.2    Narbonne, J.-F.3


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