메뉴 건너뛰기




Volumn 57, Issue 1, 1996, Pages 125-131

Effects of cadmium and environmental pollution on metallothionein and cytochrome P45O in tilapia

Author keywords

[No Author keywords available]

Indexed keywords

BENZOAPYRENE HYDROXYLASE; CYTOCHROME; ENVIRONMENTAL POLLUTION; FISH; METALLOTHIONEIN; MONOOXYGENASES; TILAPIA;

EID: 0030200457     PISSN: 00074861     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001289900165     Document Type: Article
Times cited : (26)

References (16)
  • 1
    • 0022446901 scopus 로고
    • Interaction of benzo(a)pyrene and cadmium on GSH-S-transferase and benzo(a)pyrene hydroxylase in the black sea bass Centroprisris srriara
    • Fair PH (1986) Interaction of benzo(a)pyrene and cadmium on GSH-S-transferase and benzo(a)pyrene hydroxylase in the black sea bass Centroprisris srriara. Arch Environ Contam Toxicol 15:257-263
    • (1986) Arch Environ Contam Toxicol , vol.15 , pp. 257-263
    • Fair, P.H.1
  • 2
    • 0022885797 scopus 로고
    • Biotransformation enzyme activities and histopathology in rainbow trout, Salmo gairdneri, treated with cadmium
    • Forlin L, Haux C, Karlsson-Norrgren L, Runn P, Larsson A (1986) Biotransformation enzyme activities and histopathology in rainbow trout, Salmo gairdneri, treated with cadmium. Aquat Toxicol 8:51-64
    • (1986) Aquat Toxicol , vol.8 , pp. 51-64
    • Forlin, L.1    Haux, C.2    Karlsson-Norrgren, L.3    Runn, P.4    Larsson, A.5
  • 3
    • 0024797731 scopus 로고
    • Cadmium effects on plaice liver xenobiotic and metal detoxication systems: Dose-response
    • George SG (1989) Cadmium effects on plaice liver xenobiotic and metal detoxication systems: dose-response. Aquat Toxicol 15:303-310
    • (1989) Aquat Toxicol , vol.15 , pp. 303-310
    • George, S.G.1
  • 4
    • 0022655666 scopus 로고
    • The time course of effects of cadmium and 3-methylcholanthrene on activities of enzymes of xenobiotic metabolism and metallothionein levels in the plaice, Pleuronectes platessa
    • George SG, Young P (1986) The time course of effects of cadmium and 3-methylcholanthrene on activities of enzymes of xenobiotic metabolism and metallothionein levels in the plaice, Pleuronectes platessa. Comp Biochem Physiol 83C:37-44
    • (1986) Comp Biochem Physiol , vol.83 C , pp. 37-44
    • George, S.G.1    Young, P.2
  • 5
    • 0017847465 scopus 로고
    • An improved assay of 7-ethoxycoumarin O-deethylase activity: Induction of hepatic enzyme activity in C57BL/6J and DBA/2J mice by phenobarbital, 3-methylcholanthrene and 2,3,7,8-tetrachlorodibenzo-p-dioxin
    • Greenlee WF and Poland A (1978) An improved assay of 7-ethoxycoumarin O-deethylase activity: Induction of hepatic enzyme activity in C57BL/6J and DBA/2J mice by phenobarbital, 3-methylcholanthrene and 2,3,7,8-tetrachlorodibenzo-p-dioxin. J Pharmacol Exp Ther 205:596-605
    • (1978) J Pharmacol Exp Ther , vol.205 , pp. 596-605
    • Greenlee, W.F.1    Poland, A.2
  • 7
    • 0014410265 scopus 로고
    • Substrate-inducible microsomal aryl hydrocarbon hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme
    • Nebert DW, Gelboin HV (1968) Substrate-inducible microsomal aryl hydrocarbon hydroxylase in mammalian cell culture. I. Assay and properties of induced enzyme. J Biol Chem 243:6242-6249
    • (1968) J Biol Chem , vol.243 , pp. 6242-6249
    • Nebert, D.W.1    Gelboin, H.V.2
  • 8
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature
    • Omura T, Sato R (1964) The carbon monoxide-binding pigment of liver microsomes. I. Evidence for its hemoprotein nature. J Biol Chem 239:2370-2378
    • (1964) J Biol Chem , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 9
    • 0020027597 scopus 로고
    • Comparison of metallothionein determination by polarographic and and cadmium-saturation methods
    • Onosaka S, Cherian MG (1982) Comparison of metallothionein determination by polarographic and and cadmium-saturation methods. Toxicol Appl Pharmacol 63:270-274
    • (1982) Toxicol Appl Pharmacol , vol.63 , pp. 270-274
    • Onosaka, S.1    Cherian, M.G.2
  • 10
    • 0023096696 scopus 로고
    • Review and perspective on the use of mixed-function oxygenase enzymes in biological monitoring
    • Payne JF, Fancey, LL, Rahimtula AD, Porter EL (1987) Review and perspective on the use of mixed-function oxygenase enzymes in biological monitoring. Comp Biochem Physiol 86C:233-245
    • (1987) Comp Biochem Physiol , vol.86 C , pp. 233-245
    • Payne, J.F.1    Fancey, L.L.2    Rahimtula, A.D.3    Porter, E.L.4
  • 11
    • 73849173955 scopus 로고
    • Hepatic triphosphopyridine nucleotide-cytochrome c reductase: Isolation, characterization and kinetic studies
    • Phillips JF, Langdon JR (1962) Hepatic triphosphopyridine nucleotide-cytochrome c reductase: isolation, characterization and kinetic studies. J Biol Chem 237:2652-2660.
    • (1962) J Biol Chem , vol.237 , pp. 2652-2660
    • Phillips, J.F.1    Langdon, J.R.2
  • 12
    • 0019219257 scopus 로고
    • A rapid method for assaying the metabolism of 7-ethoxyresorufin by microsomal subcellular fractions
    • Pohl R, Fouts JR (1980) A rapid method for assaying the metabolism of 7-ethoxyresorufin by microsomal subcellular fractions. Anal Biochem 107:150-155
    • (1980) Anal Biochem , vol.107 , pp. 150-155
    • Pohl, R.1    Fouts, J.R.2
  • 13
    • 0026529658 scopus 로고
    • Metallothioneins in metal regulation and toxicity in aquatic animals
    • Roesijadi G (1992) Metallothioneins in metal regulation and toxicity in aquatic animals. Aquat Toxicol 22:81-114
    • (1992) Aquat Toxicol , vol.22 , pp. 81-114
    • Roesijadi, G.1
  • 14
    • 0022610911 scopus 로고
    • Quantification of metallothionein by a silver-saturation method
    • Scheuhammer AM, Cherian MG (1986) Quantification of metallothionein by a silver-saturation method. Toxicol Appl Pharmacol 82:417-425
    • (1986) Toxicol Appl Pharmacol , vol.82 , pp. 417-425
    • Scheuhammer, A.M.1    Cherian, M.G.2
  • 15
    • 0024418612 scopus 로고
    • Cytochrome P450 forms in fish: Catalytic, immunological and sequence similarities
    • Stegeman JJ (1989) Cytochrome P450 forms in fish: catalytic, immunological and sequence similarities. Xenobiotica 19:1093-1110
    • (1989) Xenobiotica , vol.19 , pp. 1093-1110
    • Stegeman, J.J.1
  • 16
    • 0026715961 scopus 로고
    • Comparative induction of cytochrome P-450-dependent monooxygenases in the livers and gills of tilapia and carp
    • Ueng T-H, Ueng Y-F, Park SS (1992) Comparative induction of cytochrome P-450-dependent monooxygenases in the livers and gills of tilapia and carp. Aquat Toxicol 23:49-64
    • (1992) Aquat Toxicol , vol.23 , pp. 49-64
    • Ueng, T.-H.1    Ueng, Y.-F.2    Park, S.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.