메뉴 건너뛰기




Volumn 19, Issue 4, 1999, Pages 237-249

Protection from 1-cyano-3,4-epithiobutane nephrotoxicity by aminooxyacetic acid and effect on xenobiotic-metabolizing enzymes in male Fischer 344 rats

Author keywords

glutamylcysteine synthetase; 1 cyano 3,4 epithiobutane; Acivicin; Aminooxyacetic acid; Bioactivation; ECOD; EH; EROD; Glutathione; Glutathione S transferase; Nephrotoxicity; Nitrile; Probenecid; PROD

Indexed keywords

4,5 EPITHIOVALERONITRILE; ACIVICIN; AMINOOXYACETIC ACID; CYANIDE; CYSTEINE SYNTHASE; CYTOCHROME P450; EPOXIDE HYDROLASE; ETHOXYRESORUFIN DEETHYLASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; PENTOXYRESORUFIN DEALKYLASE; PROBENECID; UNCLASSIFIED DRUG; XENOBIOTIC AGENT;

EID: 0032800003     PISSN: 0260437X     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1099-1263(199907/08)19:4<237::AID-JAT569>3.0.CO;2-7     Document Type: Article
Times cited : (6)

References (60)
  • 1
    • 0024829164 scopus 로고
    • Sequential changes in hepatic and renal glutathione and development of renal karyomegaly in 1-cyano-3,4-epithiobutane toxicity in rats
    • J. L. VanSteenhouse, M. J. Fettman and D. H. Gould, Sequential changes in hepatic and renal glutathione and development of renal karyomegaly in 1-cyano-3,4-epithiobutane toxicity in rats. Food Chem. Toxicol. 27, 731-739 (1989).
    • (1989) Food Chem. Toxicol. , vol.27 , pp. 731-739
    • VanSteenhouse, J.L.1    Fettman, M.J.2    Gould, D.H.3
  • 2
    • 0025731589 scopus 로고
    • The effect of glutathione depletion by buthionine sulphoximine on 1-cyano-3,4-epithiobutane toxicity
    • J. L. VanSteenhouse, M. J. Fettman and D. H. Gould, The effect of glutathione depletion by buthionine sulphoximine on 1-cyano-3,4-epithiobutane toxicity. Food Chem. Toxicol. 9, 153-157 (1991).
    • (1991) Food Chem. Toxicol. , vol.9 , pp. 153-157
    • VanSteenhouse, J.L.1    Fettman, M.J.2    Gould, D.H.3
  • 3
  • 4
    • 0028293319 scopus 로고
    • Enzymatic repair of oxidative DNA damage
    • M. S. Satoh and T. Lindahl, Enzymatic repair of oxidative DNA damage. Cancer Res. Suppl. 54, 1899s-1901s (1994).
    • (1994) Cancer Res. Suppl. , vol.54
    • Satoh, M.S.1    Lindahl, T.2
  • 5
    • 0021691159 scopus 로고
    • Oxygen free radicals in ischemic acute renal failure in the rat
    • M. S. Paller, J. R. Hoidal and T. F. Ferris, Oxygen free radicals in ischemic acute renal failure in the rat. J. Clin. Invest. 74, 1156-1163 (1984).
    • (1984) J. Clin. Invest. , vol.74 , pp. 1156-1163
    • Paller, M.S.1    Hoidal, J.R.2    Ferris, T.F.3
  • 6
    • 0021880421 scopus 로고
    • Protection of the kidney after temporary ischemia:Free radical scavengers
    • K. Ouriel, N. G. Smedira and J. J. Ricotta, Protection of the kidney after temporary ischemia:free radical scavengers. J. Vasc. Surg. 2, 49-53 (1985).
    • (1985) J. Vasc. Surg. , vol.2 , pp. 49-53
    • Ouriel, K.1    Smedira, N.G.2    Ricotta, J.J.3
  • 7
    • 0018891998 scopus 로고
    • The inhibition of γ-glutamyl transpeptidase from human pancreatic carcinoma cells by (αs,5s)-α-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT-125; NSC-163501)
    • L. Allen, R. Meek and A. Yunis, The inhibition of γ-glutamyl transpeptidase from human pancreatic carcinoma cells by (αs,5s)-α-amino-3-chloro-4,5-dihydro-5-isoxazoleacetic acid (AT-125; NSC-163501). Res. Commun. Chem. Pathol. Pharmacol. 27, 175-182 (1980).
    • (1980) Res. Commun. Chem. Pathol. Pharmacol. , vol.27 , pp. 175-182
    • Allen, L.1    Meek, R.2    Yunis, A.3
  • 8
    • 0019023638 scopus 로고
    • Excretion of cysteine and γ-glutamylcysteine moieties in human and experimental animal γ-glutamyl transpeptidase deficiency
    • O. W. Griffith and A. Meister, Excretion of cysteine and γ-glutamylcysteine moieties in human and experimental animal γ-glutamyl transpeptidase deficiency. Proc. Natl. Acad. Sci. USA 77, 3384-3387 (1980).
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3384-3387
    • Griffith, O.W.1    Meister, A.2
  • 10
    • 2442666145 scopus 로고
    • A study, by simulataneous clearance techniques, of salicylate excretion in man. Effect of alkalinization of the urine by bicarbonate administration; effect of probenecid
    • A. B. Gutman, T. F. Yu and J. H. Sirota, A study, by simulataneous clearance techniques, of salicylate excretion in man. Effect of alkalinization of the urine by bicarbonate administration; effect of probenecid. J. Clin. Invest. 34, 711-721 (1955).
    • (1955) J. Clin. Invest. , vol.34 , pp. 711-721
    • Gutman, A.B.1    Yu, T.F.2    Sirota, J.H.3
  • 11
    • 0022970107 scopus 로고
    • In vitro studies of mechanisms of cytotoxicity
    • T. W. Jones, H. Thor and S. Orrenius. In vitro studies of mechanisms of cytotoxicity. Food Chem. Toxicol. 24, 769-773 (1986).
    • (1986) Food Chem. Toxicol. , vol.24 , pp. 769-773
    • Jones, T.W.1    Thor, H.2    Orrenius, S.3
  • 12
    • 0342635564 scopus 로고
    • Cysteine conjugate β-lyase
    • ed by W. B. Jakoby. Academic Press, New York
    • M. Tateishi and H. Shimizu, Cysteine conjugate β-lyase. In Enzymatic Basis of Detoxication, ed by W. B. Jakoby, pp. 121-130. Academic Press, New York (1980).
    • (1980) Enzymatic Basis of Detoxication , pp. 121-130
    • Tateishi, M.1    Shimizu, H.2
  • 16
    • 0026750647 scopus 로고
    • The human hepatic cytochromes P450 involved in drug metabolism
    • S. A. Wrighton and J. C. Stevens, The human hepatic cytochromes P450 involved in drug metabolism. Crit. Rev. Toxicol. 22, 1-21 (1992).
    • (1992) Crit. Rev. Toxicol. , vol.22 , pp. 1-21
    • Wrighton, S.A.1    Stevens, J.C.2
  • 17
    • 0022357068 scopus 로고
    • Ethoxy-, pentoxy, and benzyloxyphenoxazones and homologues: A series of substrates to distinguish between different induced cytochromes P-450
    • M. D. Burke, S. Thompson, C. R. Elcombe, J. Halpert, T. Haaparanta and R. T. Mayer, Ethoxy-, pentoxy, and benzyloxyphenoxazones and homologues: a series of substrates to distinguish between different induced cytochromes P-450. Biochem. Pharmacol. 34, 3337-3345 (1985).
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 3337-3345
    • Burke, M.D.1    Thompson, S.2    Elcombe, C.R.3    Halpert, J.4    Haaparanta, T.5    Mayer, R.T.6
  • 18
    • 0027264759 scopus 로고
    • The effects of inducing agents on cytochrome P450 and UDP-glucuronyltransferase activities in human HepG2 hepatoma cells
    • H. Doostdar, M. H. Grant, W. T. Melvin, C. R. Wolf and M. D. Burke, The effects of inducing agents on cytochrome P450 and UDP-glucuronyltransferase activities in human HepG2 hepatoma cells. Biochem. Pharmacol. 46, 629-635 (1993).
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 629-635
    • Doostdar, H.1    Grant, M.H.2    Melvin, W.T.3    Wolf, C.R.4    Burke, M.D.5
  • 19
    • 70450217757 scopus 로고
    • Cyanoepithioalkanes: Some chemical and toxicological studies
    • ed by D. Cavillini, G. E. Gaull and V. Zappia. Plenum Press, New York
    • J. Luthy and M. Benn, Cyanoepithioalkanes: some chemical and toxicological studies. In Natural Sulfur Compounds: Novel Biochemical and Structural Aspects, ed by D. Cavillini, G. E. Gaull and V. Zappia, pp. 381-389. Plenum Press, New York (1980).
    • (1980) Natural Sulfur Compounds: Novel Biochemical and Structural Aspects , pp. 381-389
    • Luthy, J.1    Benn, M.2
  • 20
    • 0018977364 scopus 로고
    • A convenient reverse-phase liquid chromatographic assay for epoxide hydrase
    • R. B. Westkaemper and R. P. Hanzlik, A convenient reverse-phase liquid chromatographic assay for epoxide hydrase. Anal. Biochem. 102, 63-67 (1980).
    • (1980) Anal. Biochem. , vol.102 , pp. 63-67
    • Westkaemper, R.B.1    Hanzlik, R.P.2
  • 21
    • 0342360016 scopus 로고
    • Unsuitability of the AIN 76A diet for male F-344 and CD rats and improvement by substituting starch for sucrose
    • T. E. Hamm, T. Raynor and T. Cavistin, Unsuitability of the AIN 76A diet for male F-344 and CD rats and improvement by substituting starch for sucrose. Lab. Anim. Sci. 32, 414-415 (1982).
    • (1982) Lab. Anim. Sci. , vol.32 , pp. 414-415
    • Hamm, T.E.1    Raynor, T.2    Cavistin, T.3
  • 22
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • F. Tietze, Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27, 502-522 (1969).
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 23
    • 0017395190 scopus 로고
    • γ-Glutamylcysteine synthetase: Further purification, 'half of the sites' reactivity, subunits, and specificity
    • R. Sekura and A. Meister, γ-Glutamylcysteine synthetase: further purification, 'half of the sites' reactivity, subunits, and specificity. J. Biol. Chem. 252, 2599-2605 (1977).
    • (1977) J. Biol. Chem. , vol.252 , pp. 2599-2605
    • Sekura, R.1    Meister, A.2
  • 24
    • 0016275313 scopus 로고
    • Glutathione S-transferases: The first enzymatic step in the mercapturic acid formation
    • W. H. Habig, M. J. Pabst and W. B. Jakoby, Glutathione S-transferases: the first enzymatic step in the mercapturic acid formation. J. Biol. Chem. 249, 7130-7139 (1974).
    • (1974) J. Biol. Chem. , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 25
    • 0003122802 scopus 로고
    • Preparation and characterisation of microsomal fractions for studies on xenobiotic metabolism
    • ed. by K. Snell and B. Mullock. R. L. Press, Washington, DC
    • B. G. Lake, Preparation and characterisation of microsomal fractions for studies on xenobiotic metabolism. In Biochemical Toxicology: a Practical Approach, ed. by K. Snell and B. Mullock, pp. 183-215. R. L. Press, Washington, DC. (1987).
    • (1987) Biochemical Toxicology: a Practical Approach , pp. 183-215
    • Lake, B.G.1
  • 27
    • 0023377867 scopus 로고
    • Commentary: Renal transport processes and glutathione conjugate-mediated nephrotoxicity
    • T. J. Monks and S. S. Lau, Commentary: renal transport processes and glutathione conjugate-mediated nephrotoxicity. Drug Metab. Dispos. 15, 437-441 (1987).
    • (1987) Drug Metab. Dispos. , vol.15 , pp. 437-441
    • Monks, T.J.1    Lau, S.S.2
  • 28
    • 0007276716 scopus 로고
    • Toxic nephropathy
    • ed. by B. B. Bremer and J. F. C. Rector. W. B. Saunders, Philadelphia
    • J. F. Maher, Toxic nephropathy. In The Kidney, ed. by B. B. Bremer and J. F. C. Rector, pp. 1355-1387. W. B. Saunders, Philadelphia (1976).
    • (1976) The Kidney , pp. 1355-1387
    • Maher, J.F.1
  • 29
    • 0022492563 scopus 로고
    • Mechanism of S-(1,2-dichlorovinyl)glutathione-induced nephrotoxicity
    • A. A. Elfarra, I. Jakobson and M. W. Anders, Mechanism of S-(1,2-dichlorovinyl)glutathione-induced nephrotoxicity. Biochem. Pharmacol. 35, 283-288 (1986).
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 283-288
    • Elfarra, A.A.1    Jakobson, I.2    Anders, M.W.3
  • 30
    • 0027516023 scopus 로고
    • Bioactivation of nephrotoxins and renal carcinogens by glutathione S-conjugate formation
    • W. Dekant, Bioactivation of nephrotoxins and renal carcinogens by glutathione S-conjugate formation. Toxicol. Lett. 67, 151-160 (1993).
    • (1993) Toxicol. Lett. , vol.67 , pp. 151-160
    • Dekant, W.1
  • 31
    • 0025025859 scopus 로고
    • Biosynthesis, bioactivation, and mutagenicity of S-conjugates
    • W. Dekant, S. Vamvakas and M. W. Anders, Biosynthesis, bioactivation, and mutagenicity of S-conjugates. Toxicol. Lett. 53, 53-58 (1990).
    • (1990) Toxicol. Lett. , vol.53 , pp. 53-58
    • Dekant, W.1    Vamvakas, S.2    Anders, M.W.3
  • 32
    • 0022380437 scopus 로고
    • Glutathione conjugates of 2-bromohydroquinone are nephrotoxic
    • T. J. Monks, S. S. Lau, R. J. Highet and J. R. Gillette, Glutathione conjugates of 2-bromohydroquinone are nephrotoxic. Drug Metab. Dispos. 13, 553-559 (1985).
    • (1985) Drug Metab. Dispos , vol.13 , pp. 553-559
    • Monks, T.J.1    Lau, S.S.2    Highet, R.J.3    Gillette, J.R.4
  • 33
    • 0021167919 scopus 로고
    • Organic ion transport during seven decades. The amino acids
    • H. N. Christensen, Organic ion transport during seven decades. The amino acids. Biochim. Biophys. Acta 779, 255-269 (1984).
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 255-269
    • Christensen, H.N.1
  • 34
    • 0022638764 scopus 로고
    • Role of membrane transport in metabolism and function of glutathione in mammals
    • S. Bannai and N. Tateishi, Role of membrane transport in metabolism and function of glutathione in mammals. J. Membr. Biol. 89, 1-8 (1986).
    • (1986) J. Membr. Biol. , vol.89 , pp. 1-8
    • Bannai, S.1    Tateishi, N.2
  • 35
    • 0018963749 scopus 로고
    • Transport interaction of L-cysteine and L-glutamate in human diploid fibroblasts in culture
    • S. Bannai, and E. Kitamura, Transport interaction of L-cysteine and L-glutamate in human diploid fibroblasts in culture. J. Biol. Chem. 255, 115-120 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 115-120
    • Bannai, S.1    Kitamura, E.2
  • 36
    • 0019410188 scopus 로고
    • Role of proton dissociation in the transport of cystine and glutamate in human diploid fibroblasts in culture
    • S. Bannai and E. Kitamura, Role of proton dissociation in the transport of cystine and glutamate in human diploid fibroblasts in culture. J. Biol. Chem. 256, 5770-5772 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 5770-5772
    • Bannai, S.1    Kitamura, E.2
  • 37
    • 0020316977 scopus 로고
    • Contrasts in transport systems for anionic amino acids in hepatocytes and a hepatoma cell line HTC
    • M. Makowske and H. N. Christensen, Contrasts in transport systems for anionic amino acids in hepatocytes and a hepatoma cell line HTC. J. Biol. Chem. 257, 5663-5670 (1982).
    • (1982) J. Biol. Chem , vol.257 , pp. 5663-5670
    • Makowske, M.1    Christensen, H.N.2
  • 38
    • 0024432603 scopus 로고
    • Regulation of cellular glutathione
    • S. M. Deneke and B. L. Fanburg, Regulation of cellular glutathione. Am. J. Physiol. 257, L163-L173 (1989).
    • (1989) Am. J. Physiol. , vol.257
    • Deneke, S.M.1    Fanburg, B.L.2
  • 39
    • 0027485217 scopus 로고
    • Differential effect of cyanohydroxybutene on glutathione synthesis in liver and pancreas of male rats
    • M. A. Davis, M. A. Wallig, D. Eaton, K. I. Borroz and E. H. Jeffery, Differential effect of cyanohydroxybutene on glutathione synthesis in liver and pancreas of male rats. Toxicol. Appl. Pharmacol. 123, 257-264 (1993).
    • (1993) Toxicol. Appl. Pharmacol. , vol.123 , pp. 257-264
    • Davis, M.A.1    Wallig, M.A.2    Eaton, D.3    Borroz, K.I.4    Jeffery, E.H.5
  • 40
    • 0018894208 scopus 로고
    • Adenocarcinoma of the kidney. III. Histogenesis of renal adenocarcinomas induced in rats by N-(4′-fluoro-4-biphenylyl) acetamide
    • J. H. Dees, B. M. Heatfield, M. D. Reuber and B. F. Trump, Adenocarcinoma of the kidney. III. Histogenesis of renal adenocarcinomas induced in rats by N-(4′-fluoro-4-biphenylyl) acetamide. J. Natl. Cancer Inst. 64, 1537-1541 (1980).
    • (1980) J. Natl. Cancer Inst. , vol.64 , pp. 1537-1541
    • Dees, J.H.1    Heatfield, B.M.2    Reuber, M.D.3    Trump, B.F.4
  • 41
    • 0018821140 scopus 로고
    • Adenocarcinoma of the kidney. IV. Electron microscopic study of the development of renal adenocarcinomas induced in rats by by N-(4′-fluoro-4-biphenylyl) acetamide
    • J. H. Dees, B. M. Heatfield, M. D. Reuber and B. F. Trump, Adenocarcinoma of the kidney. IV. Electron microscopic study of the development of renal adenocarcinomas induced in rats by by N-(4′-fluoro-4-biphenylyl) acetamide. J. Natl. Cancer Inst. 64, 1547-1551 (1980).
    • (1980) J. Natl. Cancer Inst. , vol.64 , pp. 1547-1551
    • Dees, J.H.1    Heatfield, B.M.2    Reuber, M.D.3    Trump, B.F.4
  • 42
    • 0021747901 scopus 로고
    • Morphologic changes in rat urothelial cells during carcinogenesis: II. Image cytometry
    • I. T. Young, M. Vanderlaan, L. Kromhout, R. Jensen, A. Grover and E. King, Morphologic changes in rat urothelial cells during carcinogenesis: II. Image cytometry. Cytometry 5, 454-462 (1984).
    • (1984) Cytometry , vol.5 , pp. 454-462
    • Young, I.T.1    Vanderlaan, M.2    Kromhout, L.3    Jensen, R.4    Grover, A.5    King, E.6
  • 43
    • 0015290038 scopus 로고
    • Cell proliferation in rat kidney induced by lead acetate and effects of uninephrectomy on the proliferation
    • D. D. Choie and G. W. Richter, Cell proliferation in rat kidney induced by lead acetate and effects of uninephrectomy on the proliferation. Am. J. Pathol. 66, 265-275 (1972).
    • (1972) Am. J. Pathol. , vol.66 , pp. 265-275
    • Choie, D.D.1    Richter, G.W.2
  • 44
    • 0016228063 scopus 로고
    • Nuclear cytochemical alterations in α-protein-induced nephrocytomegalia
    • J. P. Reyniers, J. C. Woodard and M. R. Alvarez, Nuclear cytochemical alterations in α-protein-induced nephrocytomegalia. Lab. Invest. 30, 582-588 (1974).
    • (1974) Lab. Invest. , vol.30 , pp. 582-588
    • Reyniers, J.P.1    Woodard, J.C.2    Alvarez, M.R.3
  • 46
    • 0024491072 scopus 로고
    • Biosynthesis and degradation of methylglyoxal in animals
    • S. Ohmori, M. Mori, K. Shiraha and M. Kawase, Biosynthesis and degradation of methylglyoxal in animals. Prog. Clin. Biol. Res. 290, 397-412 (1989).
    • (1989) Prog. Clin. Biol. Res. , vol.290 , pp. 397-412
    • Ohmori, S.1    Mori, M.2    Shiraha, K.3    Kawase, M.4
  • 47
    • 0002074019 scopus 로고
    • Cell division and cancer
    • A. Szent-Gyorgyi, Cell division and cancer. Science 149, 34-37 (1965).
    • (1965) Science , vol.149 , pp. 34-37
    • Szent-Gyorgyi, A.1
  • 48
    • 0025202783 scopus 로고
    • Enhancing effect of S-(1,2-dicarboxyethyl)glutathione on epidermal growth factor-stimulated DNA synthesis in primary cultures of adult rat hepatocytes
    • M. Miyazaki, L. Bai, S. Tsuboi, S. Ohmori, K. Ogata, J. Sato and M. Namba, Enhancing effect of S-(1,2-dicarboxyethyl)glutathione on epidermal growth factor-stimulated DNA synthesis in primary cultures of adult rat hepatocytes. Res. Exp. Med. 190, 381-387 (1990).
    • (1990) Res. Exp. Med. , vol.190 , pp. 381-387
    • Miyazaki, M.1    Bai, L.2    Tsuboi, S.3    Ohmori, S.4    Ogata, K.5    Sato, J.6    Namba, M.7
  • 49
    • 0024269217 scopus 로고
    • Glutathione S-transferases: Structural and catalytic activity
    • B. Mannervik and U. H. Danielson, Glutathione S-transferases: structural and catalytic activity. CRC Crit. Rev. Biochem. 23, 283-337 (1988).
    • (1988) CRC Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 50
    • 0027365971 scopus 로고
    • Isozyme specificity of novel glutathione S-transferase inhibitors
    • J. E. Flatguard, K. E. Bauer and L. M. Kauvar, Isozyme specificity of novel glutathione S-transferase inhibitors. Cancer Chemother. Pharmacol. 33, 63-70 (1993).
    • (1993) Cancer Chemother. Pharmacol. , vol.33 , pp. 63-70
    • Flatguard, J.E.1    Bauer, K.E.2    Kauvar, L.M.3
  • 51
    • 0025150771 scopus 로고
    • Inhibition of rat and human glutathione S-transferase isoenzymes by ethycrynic acid and its glutathione conjugate
    • J. H. T. M. Ploeman, B. van Ommen and P. J. van Bladeren, Inhibition of rat and human glutathione S-transferase isoenzymes by ethycrynic acid and its glutathione conjugate. Biochem. Pharmacol. 40, 1631-1635 (1991).
    • (1991) Biochem. Pharmacol. , vol.40 , pp. 1631-1635
    • Ploeman, J.H.T.M.1    Van Ommen, B.2    Van Bladeren, P.J.3
  • 55
    • 0023100690 scopus 로고
    • Formation of glutathione-conjugated semiquinones by the reaction of quinones with glutathione: An ESR study
    • N. Takahashi, J. Schreiber, F. Volker and R. P. Mason, Formation of glutathione-conjugated semiquinones by the reaction of quinones with glutathione: an ESR study. Arch. Biochem. Biophys. 252, 41-48 (1987).
    • (1987) Arch. Biochem. Biophys. , vol.252 , pp. 41-48
    • Takahashi, N.1    Schreiber, J.2    Volker, F.3    Mason, R.P.4
  • 56
    • 0001891285 scopus 로고
    • Comparison of and relationships between glutathione S-transferase and cytocrome P-450 systems
    • ed. by H. Sies and B. Ketterer. Academic Press, San Diego
    • L. A. Peterson and F. P. Guengerich, Comparison of and relationships between glutathione S-transferase and cytocrome P-450 systems. In Glutathione Conjugation: Mechanisms and Biological Significance, ed. by H. Sies and B. Ketterer, pp. 193-233. Academic Press, San Diego (1988).
    • (1988) Glutathione Conjugation: Mechanisms and Biological Significance , pp. 193-233
    • Peterson, L.A.1    Guengerich, F.P.2
  • 57
    • 0025027375 scopus 로고
    • A comparison of hepatic P450 induction in rat and trout (Oncorhynchus mykiss): Delineation of the site of resistance of fish to phenobarbital-type inducers
    • K. M. Kleinow, M. L Haasch, D. E. Williams and J. J. Lech, A comparison of hepatic P450 induction in rat and trout (Oncorhynchus mykiss): delineation of the site of resistance of fish to phenobarbital-type inducers. Comp. Biochem. Physiol. C Pharmacol. Toxicol. Endocrinol. 96, 259-270 (1990).
    • (1990) Comp. Biochem. Physiol. C Pharmacol. Toxicol. Endocrinol. , vol.96 , pp. 259-270
    • Kleinow, K.M.1    Haasch, M.L.2    Williams, D.E.3    Lech, J.J.4
  • 58
    • 0025344378 scopus 로고
    • Cytochrome P450 isoenzymes, epoxide hydrolase, and glutathione transferases in rat and human hepatic and extrahepatic tissues
    • I. de Waziers, P. H. Cugnenc, C. S. Yang, J. P. Leroux and P. H. Beaune, Cytochrome P450 isoenzymes, epoxide hydrolase, and glutathione transferases in rat and human hepatic and extrahepatic tissues. J. Pharmacol. Exp Ther. 253, 387-394 (1990).
    • (1990) J. Pharmacol. Exp Ther. , vol.253 , pp. 387-394
    • De Waziers, I.1    Cugnenc, P.H.2    Yang, C.S.3    Leroux, J.P.4    Beaune, P.H.5
  • 59
    • 0344036796 scopus 로고
    • Crude commercial diets induce hepatic cytochrome P-450 systems
    • L. B. Deloria and G. J. Mannering, Crude commercial diets induce hepatic cytochrome P-450 systems. Pharmacologist 28, 214 (1986).
    • (1986) Pharmacologist 28 , pp. 214
    • Deloria, L.B.1    Mannering, G.J.2
  • 60
    • 0028943584 scopus 로고
    • Substrate-dependent competition of different P450 isozymes for limiting NADPH-cytochrome P450 reductase
    • G. F. Cawley, C. J. Batie and W. L. Backes, Substrate-dependent competition of different P450 isozymes for limiting NADPH-cytochrome P450 reductase. Biochemistry 34, 1244-1247 (1995).
    • (1995) Biochemistry , vol.34 , pp. 1244-1247
    • Cawley, G.F.1    Batie, C.J.2    Backes, W.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.