메뉴 건너뛰기




Volumn , Issue , 2003, Pages 117-185

Development of Antioxidant and Xenobiotic Metabolizing Enzyme Systems

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84942244891     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-012324751-3/50046-2     Document Type: Chapter
Times cited : (6)

References (103)
  • 1
  • 2
    • 0000800579 scopus 로고    scopus 로고
    • Pulmonary developmental responses to toxicants
    • Elsevier Science, Inc., New York, R.A. Roth (Ed.) Toxicology of the Respiratory System
    • Fanucchi M, Plopper C Pulmonary developmental responses to toxicants. Comprehensive Toxicology 1997, 203-220. Elsevier Science, Inc., New York. 1st Edition. R.A. Roth (Ed.).
    • (1997) Comprehensive Toxicology , pp. 203-220
    • Fanucchi, M.1    Plopper, C.2
  • 3
    • 0028855791 scopus 로고
    • Relationship of cytochrome P450 activity to Clara cell cytotoxicity. IV. Metabolism of naphthalene and naphthalene oxide in microdissected airways from mice, rats, and hamsters
    • Buckpitt A, Chang AM, Weir A, et al. Relationship of cytochrome P450 activity to Clara cell cytotoxicity. IV. Metabolism of naphthalene and naphthalene oxide in microdissected airways from mice, rats, and hamsters. Mol. Pharmacol. 1995, 47:74-81.
    • (1995) Mol. Pharmacol. , vol.47 , pp. 74-81
    • Buckpitt, A.1    Chang, A.M.2    Weir, A.3
  • 4
    • 0027362757 scopus 로고
    • 1-Nitronaphthalene toxicity in rat lung and liver: effects of inhibiting and inducing cytochrome P450 activity
    • Verschoyle RD, Carthew P, Wolf CR, et al. 1-Nitronaphthalene toxicity in rat lung and liver: effects of inhibiting and inducing cytochrome P450 activity. Toxicol. Appl. Pharmacol. 1993, 122:208-213.
    • (1993) Toxicol. Appl. Pharmacol. , vol.122 , pp. 208-213
    • Verschoyle, R.D.1    Carthew, P.2    Wolf, C.R.3
  • 5
    • 0024503222 scopus 로고
    • Relationship of naphthalene and 2-methylnaphthalene metabolism to pulmonary bronchiolar epithelial cell necrosis
    • Buckpitt AR, Franklin RB Relationship of naphthalene and 2-methylnaphthalene metabolism to pulmonary bronchiolar epithelial cell necrosis. Pharmacol. Ther. 1989, 41:393-410.
    • (1989) Pharmacol. Ther. , vol.41 , pp. 393-410
    • Buckpitt, A.R.1    Franklin, R.B.2
  • 6
    • 0020056033 scopus 로고
    • Distribution and metabolism of the pulmonary alkylating agent and cytotoxin, 4-ipomeanol, in control and diethylmaleate-treated rats
    • Statham CN, Boyd MR Distribution and metabolism of the pulmonary alkylating agent and cytotoxin, 4-ipomeanol, in control and diethylmaleate-treated rats. Biochem. Pharmacol. 1982, 31:1585-1589.
    • (1982) Biochem. Pharmacol. , vol.31 , pp. 1585-1589
    • Statham, C.N.1    Boyd, M.R.2
  • 7
    • 0018595843 scopus 로고
    • Species and strain differences in target organ alkylation and toxicity by 4-ipomeanol. Predictive value of covalent binding in studies of target organ toxicities by reactive metabolites
    • Dutcher JS, Boyd MR Species and strain differences in target organ alkylation and toxicity by 4-ipomeanol. Predictive value of covalent binding in studies of target organ toxicities by reactive metabolites. Biochem. Pharmacol. 1979, 28:3367-3372.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 3367-3372
    • Dutcher, J.S.1    Boyd, M.R.2
  • 8
    • 0018824250 scopus 로고
    • The pulmonary Clara cell as a target for toxic chemicals requiring metabolic activation; studies with carbon tetrachloride
    • Boyd MR, Statham CN, Longo NS The pulmonary Clara cell as a target for toxic chemicals requiring metabolic activation; studies with carbon tetrachloride. J. Pharmacol. Exp. Ther. 1980, 212:109-114.
    • (1980) J. Pharmacol. Exp. Ther. , vol.212 , pp. 109-114
    • Boyd, M.R.1    Statham, C.N.2    Longo, N.S.3
  • 9
    • 0026511385 scopus 로고
    • 1,1-Dichloroethylene-induced alterations in glutathione and covalent binding in murine lung: morphological, histochemical, and biochemical studies
    • Moussa M, Forkert PG 1,1-Dichloroethylene-induced alterations in glutathione and covalent binding in murine lung: morphological, histochemical, and biochemical studies. J. Pathol. 1992, 166:199-207.
    • (1992) J. Pathol. , vol.166 , pp. 199-207
    • Moussa, M.1    Forkert, P.G.2
  • 10
    • 0015860727 scopus 로고
    • Metabolism and binding of aromatic hydrocarbons in the lung. Relationship to experimental bronchiolar necrosis
    • Reid WD, Ilett KF, Glick JM, et al. Metabolism and binding of aromatic hydrocarbons in the lung. Relationship to experimental bronchiolar necrosis. Am. Rev. Respir. Dis. 1973, 107:539-551.
    • (1973) Am. Rev. Respir. Dis. , vol.107 , pp. 539-551
    • Reid, W.D.1    Ilett, K.F.2    Glick, J.M.3
  • 11
    • 0025247795 scopus 로고
    • Organ-selective switching of 3-methylindole toxicity by glutathione depletion
    • Yost GS, Kuntz DJ, McGill LD Organ-selective switching of 3-methylindole toxicity by glutathione depletion. Toxicol. Appl. Pharmacol. 1990, 103:40-51.
    • (1990) Toxicol. Appl. Pharmacol. , vol.103 , pp. 40-51
    • Yost, G.S.1    Kuntz, D.J.2    McGill, L.D.3
  • 12
    • 0022403125 scopus 로고
    • Adducts of 3-methylindole and glutathione: species differences in organ-selective bioactivation
    • Nocerini MR, Carlson JR, Yost GS Adducts of 3-methylindole and glutathione: species differences in organ-selective bioactivation. Toxicol. Lett. 1985, 28:79-87.
    • (1985) Toxicol. Lett. , vol.28 , pp. 79-87
    • Nocerini, M.R.1    Carlson, J.R.2    Yost, G.S.3
  • 13
    • 0023681277 scopus 로고
    • Glutathione monoethyl ester can selectively protect liver from high dose BCNU or cyclophosphamide
    • Teicher BA, Crawford JM, Holden SA, et al. Glutathione monoethyl ester can selectively protect liver from high dose BCNU or cyclophosphamide. Cancer 1988, 62:1275-1281.
    • (1988) Cancer , vol.62 , pp. 1275-1281
    • Teicher, B.A.1    Crawford, J.M.2    Holden, S.A.3
  • 14
    • 0019139164 scopus 로고
    • Toxic effects of methylcyclopentadienyl manganese tricarbonyl (MMT) in rats: role of metabolism
    • Hanzlik RP, Stitt R, Traiger GJ Toxic effects of methylcyclopentadienyl manganese tricarbonyl (MMT) in rats: role of metabolism. Toxicol. Appl. Pharmacol. 1980, 56:353-360.
    • (1980) Toxicol. Appl. Pharmacol. , vol.56 , pp. 353-360
    • Hanzlik, R.P.1    Stitt, R.2    Traiger, G.J.3
  • 15
    • 0019773308 scopus 로고
    • Modification by phenobarbital of chlorphentermine-induced changes in lung morphology and drug-metabolizing enzymes in new-born rats
    • Kacew S, Parulekar MR, Narbaitz R, et al. Modification by phenobarbital of chlorphentermine-induced changes in lung morphology and drug-metabolizing enzymes in new-born rats. J. Toxicol. Environ. Health 1981, 8:873-884.
    • (1981) J. Toxicol. Environ. Health , vol.8 , pp. 873-884
    • Kacew, S.1    Parulekar, M.R.2    Narbaitz, R.3
  • 16
    • 0026663195 scopus 로고
    • Catalase, superoxide dismutase and glutathione peroxidase activities of lung and liver during human development
    • McElroy MC, Postle AD, Kelly FJ Catalase, superoxide dismutase and glutathione peroxidase activities of lung and liver during human development. Biochim. Biophys. Acta 1992, 1117:153-158.
    • (1992) Biochim. Biophys. Acta , vol.1117 , pp. 153-158
    • McElroy, M.C.1    Postle, A.D.2    Kelly, F.J.3
  • 17
    • 0026808952 scopus 로고
    • Rat lung antioxidant enzymes: differences in perinatal gene expression and regulation
    • Clerch LB, Massaro D Rat lung antioxidant enzymes: differences in perinatal gene expression and regulation. Am. J. Physiol. 1992, 263:L466-L470.
    • (1992) Am. J. Physiol. , vol.263 , pp. L466-L470
    • Clerch, L.B.1    Massaro, D.2
  • 18
    • 0025728775 scopus 로고
    • Immunohistochemical study on perinatal development of rat superoxide dismutases in lungs and kidneys
    • Asayama K, Hayashibe H, Dobashi K, et al. Immunohistochemical study on perinatal development of rat superoxide dismutases in lungs and kidneys. Pediatr. Res. 1991, 29:487-491.
    • (1991) Pediatr. Res. , vol.29 , pp. 487-491
    • Asayama, K.1    Hayashibe, H.2    Dobashi, K.3
  • 19
    • 0023200961 scopus 로고
    • Development of lung antioxidant enzyme system in late gestation: possible implications for the prematurely born infant
    • Frank L, Sosenko IR Development of lung antioxidant enzyme system in late gestation: possible implications for the prematurely born infant. J. Pediatr. 1987, 110:9-14.
    • (1987) J. Pediatr. , vol.110 , pp. 9-14
    • Frank, L.1    Sosenko, I.R.2
  • 20
    • 0025308446 scopus 로고
    • Prenatal development of antioxidant enzymes in rat lung, kidney, and heart: marked increase in immunoreactive superoxide dismutases, glutathione peroxidase, and catalase in the kidney
    • Hayashibe H, Asayama K, Dobashi K, et al. Prenatal development of antioxidant enzymes in rat lung, kidney, and heart: marked increase in immunoreactive superoxide dismutases, glutathione peroxidase, and catalase in the kidney. Pediatr. Res. 1990, 27:472-475.
    • (1990) Pediatr. Res. , vol.27 , pp. 472-475
    • Hayashibe, H.1    Asayama, K.2    Dobashi, K.3
  • 21
    • 0029738975 scopus 로고    scopus 로고
    • Possible mechanism for late gestational development of the antioxidant enzymes in the fetal rat lung
    • Frank L, Price LT, Whitney PL Possible mechanism for late gestational development of the antioxidant enzymes in the fetal rat lung. Biol. Neonate 1996, 70:116-127.
    • (1996) Biol. Neonate , vol.70 , pp. 116-127
    • Frank, L.1    Price, L.T.2    Whitney, P.L.3
  • 22
    • 0025058208 scopus 로고
    • Developmental expression of antioxidant enzymes in guinea pig lung and liver
    • Rickett GM, Kelly FJ Developmental expression of antioxidant enzymes in guinea pig lung and liver. Development 1990, 108:331-336.
    • (1990) Development , vol.108 , pp. 331-336
    • Rickett, G.M.1    Kelly, F.J.2
  • 23
    • 0024446112 scopus 로고
    • Thyroid inhibition and developmental increases in fetal rat lung antioxidant enzymes
    • Sosenko IR, Frank L Thyroid inhibition and developmental increases in fetal rat lung antioxidant enzymes. Am. J. Physiol. 1989, 257:L94-L99.
    • (1989) Am. J. Physiol. , vol.257 , pp. L94-L99
    • Sosenko, I.R.1    Frank, L.2
  • 24
    • 0022998151 scopus 로고
    • Hormonal and local factors influence antioxidant enzyme activity of rat fetal lung cells in vitro
    • Tanswell AK, Tzaki MG, Byrne PJ Hormonal and local factors influence antioxidant enzyme activity of rat fetal lung cells in vitro. Exp. Lung. Res. 1986, 11:49-59.
    • (1986) Exp. Lung. Res. , vol.11 , pp. 49-59
    • Tanswell, A.K.1    Tzaki, M.G.2    Byrne, P.J.3
  • 25
    • 0026334987 scopus 로고
    • Corticosteroids, thyrotropin-releasing hormone, and antioxidant enzymes in preterm lamb lungs
    • Walther FJ, Ikegami M, Warburton D, et al. Corticosteroids, thyrotropin-releasing hormone, and antioxidant enzymes in preterm lamb lungs. Pediatr. Res. 1991, 30:518-521.
    • (1991) Pediatr. Res. , vol.30 , pp. 518-521
    • Walther, F.J.1    Ikegami, M.2    Warburton, D.3
  • 26
    • 0015848173 scopus 로고
    • Superoxide dismutase. Organelle specificity
    • Weisiger RA, Fridovich I Superoxide dismutase. Organelle specificity. J. Biol. Chem. 1973, 248:3582-3592.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 27
    • 0015694842 scopus 로고
    • Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial localization
    • Weisiger RA, Fridovich I Mitochondrial superoxide dismutase. Site of synthesis and intramitochondrial localization. J. Biol. Chem. 1973, 248:4793-4796.
    • (1973) J. Biol. Chem. , vol.248 , pp. 4793-4796
    • Weisiger, R.A.1    Fridovich, I.2
  • 28
    • 0026476480 scopus 로고
    • Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells
    • Crapo JD, Oury T, Rabouille C, et al. Copper, zinc superoxide dismutase is primarily a cytosolic protein in human cells. Proc. Natl. Acad. Sci. USA 1992, 89:10405-10409.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10405-10409
    • Crapo, J.D.1    Oury, T.2    Rabouille, C.3
  • 29
    • 0021745377 scopus 로고
    • Extracellular superoxide dismutase in human tissues and human cell lines
    • Marklund SL Extracellular superoxide dismutase in human tissues and human cell lines. J. Clin. Invest. 1984, 74:1398-1403.
    • (1984) J. Clin. Invest. , vol.74 , pp. 1398-1403
    • Marklund, S.L.1
  • 30
    • 0030014041 scopus 로고    scopus 로고
    • Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase
    • Oury TD, Crapo JD, Valnickova Z, et al. Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase. Biochem. J. 1996, 317:51-57.
    • (1996) Biochem. J. , vol.317 , pp. 51-57
    • Oury, T.D.1    Crapo, J.D.2    Valnickova, Z.3
  • 33
    • 0021611710 scopus 로고
    • Differentiation-arrested rat fetal lung in primary monolayer cell culture. III. Antioxidant enzyme activity
    • Tanswell AK, Freeman BA Differentiation-arrested rat fetal lung in primary monolayer cell culture. III. Antioxidant enzyme activity. Exp. Lung Res. 1984, 6:149-158.
    • (1984) Exp. Lung Res. , vol.6 , pp. 149-158
    • Tanswell, A.K.1    Freeman, B.A.2
  • 34
    • 0023656038 scopus 로고
    • Developmental regulation of rat lung Cu, Zn-superoxide dismutase
    • Hass MA, Massaro D Developmental regulation of rat lung Cu, Zn-superoxide dismutase. Biochem. J. 1987, 246:697-703.
    • (1987) Biochem. J. , vol.246 , pp. 697-703
    • Hass, M.A.1    Massaro, D.2
  • 35
    • 0022473426 scopus 로고
    • Neonatal developmental pattern of superoxide dismutase and aniline hydroxylase in rat lung
    • Kakkar P, Jaffery FN, Viswanathan PN Neonatal developmental pattern of superoxide dismutase and aniline hydroxylase in rat lung. Environ. Res. 1986, 41:302-308.
    • (1986) Environ. Res. , vol.41 , pp. 302-308
    • Kakkar, P.1    Jaffery, F.N.2    Viswanathan, P.N.3
  • 36
    • 0027212449 scopus 로고
    • Differential gene expression of antioxidant enzymes in the perinatal rat lung
    • Chen Y, Frank L Differential gene expression of antioxidant enzymes in the perinatal rat lung. Pediatr. Res. 1993, 34:27-31.
    • (1993) Pediatr. Res. , vol.34 , pp. 27-31
    • Chen, Y.1    Frank, L.2
  • 37
    • 0027955869 scopus 로고
    • Expression of copper/zinc superoxide dismutase and glutathione peroxidase in organs of developing mouse embryos, fetuses, and neonates
    • de Haan JB, Tymms MJ, Cristiano F, et al. Expression of copper/zinc superoxide dismutase and glutathione peroxidase in organs of developing mouse embryos, fetuses, and neonates. Pediatr. Res. 1994, 35:188-196.
    • (1994) Pediatr. Res. , vol.35 , pp. 188-196
    • de Haan, J.B.1    Tymms, M.J.2    Cristiano, F.3
  • 38
    • 0023857191 scopus 로고
    • Studies on the expression of Cu, Zn superoxide dismutase in human tissues during development
    • Strange RC, Cotton W, Fryer AA, et al. Studies on the expression of Cu, Zn superoxide dismutase in human tissues during development. Biochim. Biophys. Acta 1988, 964:260-265.
    • (1988) Biochim. Biophys. Acta , vol.964 , pp. 260-265
    • Strange, R.C.1    Cotton, W.2    Fryer, A.A.3
  • 39
    • 0025176655 scopus 로고
    • Postnatal development of enzyme activities associated with protection against oxidative stress in the mouse
    • Harman AW, McKenna M, Adamson GM Postnatal development of enzyme activities associated with protection against oxidative stress in the mouse. Biol. Neonate 1990, 57:187-193.
    • (1990) Biol. Neonate , vol.57 , pp. 187-193
    • Harman, A.W.1    McKenna, M.2    Adamson, G.M.3
  • 40
    • 0026085224 scopus 로고
    • Developmental aspects of experimental pulmonary oxygen toxicity
    • Frank L Developmental aspects of experimental pulmonary oxygen toxicity. Free Radic. Biol. Med. 1991, 11:463-494.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 463-494
    • Frank, L.1
  • 41
    • 0024537409 scopus 로고
    • Metabolism of benzo[a]pyrene and 7 beta, 8 alpha-dihydroxy-9 alpha, 10 alpha-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene in lung and liver of newborn mice
    • Melikian AA, Bagheri K, Hecht SS, et al. Metabolism of benzo[a]pyrene and 7 beta, 8 alpha-dihydroxy-9 alpha, 10 alpha-epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene in lung and liver of newborn mice. Chem-Biol. Interact. 1989, 69:245-257.
    • (1989) Chem-Biol. Interact. , vol.69 , pp. 245-257
    • Melikian, A.A.1    Bagheri, K.2    Hecht, S.S.3
  • 43
    • 0020537304 scopus 로고
    • Selective modification of glutathione metabolism
    • Meister A Selective modification of glutathione metabolism. Science 1983, 220:472-477.
    • (1983) Science , vol.220 , pp. 472-477
    • Meister, A.1
  • 44
    • 0016228060 scopus 로고
    • Glutathione, metabolism and function via the gamma-glutamyl cycle
    • Meister A Glutathione, metabolism and function via the gamma-glutamyl cycle. Life Sci. 1974, 15:177-190.
    • (1974) Life Sci. , vol.15 , pp. 177-190
    • Meister, A.1
  • 45
    • 0024432603 scopus 로고
    • Regulation of cellular glutathione
    • Deneke SM, Fanburg BL Regulation of cellular glutathione. Am. J. Physiol. 1989, 257:L163-L173.
    • (1989) Am. J. Physiol. , vol.257 , pp. L163-L173
    • Deneke, S.M.1    Fanburg, B.L.2
  • 46
    • 0026004832 scopus 로고
    • Inhibition of glutathione synthesis in the newborn rat: a model for endogenously produced oxidative stress
    • Martensson J, Jain A, Stole E, et al. Inhibition of glutathione synthesis in the newborn rat: a model for endogenously produced oxidative stress. Proc. Natl. Acad. Sci. USA 1991, 88:9360-9364.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9360-9364
    • Martensson, J.1    Jain, A.2    Stole, E.3
  • 47
    • 0030977910 scopus 로고    scopus 로고
    • Ontogeny of gamma-glutamyltransferase in the rat lung
    • Oakes SM, Takahashi Y, Williams MC, et al. Ontogeny of gamma-glutamyltransferase in the rat lung. Am. J. Physiol. 1997, 272:L739-L744.
    • (1997) Am. J. Physiol. , vol.272 , pp. L739-L744
    • Oakes, S.M.1    Takahashi, Y.2    Williams, M.C.3
  • 48
    • 0028911892 scopus 로고
    • Enzymes of the gamma-glutamyl cycle are programmed in utero by maternal nutrition
    • Langley-Evans SC, Wood S, Jackson AA Enzymes of the gamma-glutamyl cycle are programmed in utero by maternal nutrition. Ann. Nutr. Metab. 1995, 39:28-35.
    • (1995) Ann. Nutr. Metab. , vol.39 , pp. 28-35
    • Langley-Evans, S.C.1    Wood, S.2    Jackson, A.A.3
  • 49
    • 0032899924 scopus 로고    scopus 로고
    • Glutathione synthetic activity in the lungs in newborn guinea pigs
    • Lavoie JC, Spalinger M, Chessex P Glutathione synthetic activity in the lungs in newborn guinea pigs. Lung 1999, 177:1-7.
    • (1999) Lung , vol.177 , pp. 1-7
    • Lavoie, J.C.1    Spalinger, M.2    Chessex, P.3
  • 50
    • 0023923526 scopus 로고
    • Role of transferrin and ceruloplasmin in antioxidant activity of lung epithelial lining fluid
    • Pacht ER, Davis WB Role of transferrin and ceruloplasmin in antioxidant activity of lung epithelial lining fluid. J. Appl. Physiol. 1988, 64:2092-2099.
    • (1988) J. Appl. Physiol. , vol.64 , pp. 2092-2099
    • Pacht, E.R.1    Davis, W.B.2
  • 51
    • 0030075742 scopus 로고    scopus 로고
    • Cellular expression of ceruloplasmin in baboon and mouse lung during development and inflammation
    • Yang F, Friedrichs WE, deGraffenried L, et al. Cellular expression of ceruloplasmin in baboon and mouse lung during development and inflammation. Am. J. Respir. Cell Mol. Biol. 1996, 14:161-169.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.14 , pp. 161-169
    • Yang, F.1    Friedrichs, W.E.2    deGraffenried, L.3
  • 52
    • 0034872152 scopus 로고    scopus 로고
    • Induction of peroxiredoxin gene expression by oxygen in lungs of newborn primates
    • Das KC, Pahl PM, Guo XL, et al. Induction of peroxiredoxin gene expression by oxygen in lungs of newborn primates. Am. J. Respir. Cell Mol. Biol. 2001, 25:226-232.
    • (2001) Am. J. Respir. Cell Mol. Biol. , vol.25 , pp. 226-232
    • Das, K.C.1    Pahl, P.M.2    Guo, X.L.3
  • 53
    • 0035105863 scopus 로고    scopus 로고
    • Ascorbate acid concentration in airways lining fluid from infants who develop chronic lung disease of prematurity
    • Vyas JR, Currie A, Dunster C, et al. Ascorbate acid concentration in airways lining fluid from infants who develop chronic lung disease of prematurity. Eur. J. Pediatr. 2001, 160:177-184.
    • (2001) Eur. J. Pediatr. , vol.160 , pp. 177-184
    • Vyas, J.R.1    Currie, A.2    Dunster, C.3
  • 54
    • 0027257599 scopus 로고
    • Postnatal changes in the expression and distribution of pulmonary cytochrome P450 monooxygenases during Clara cell differentiation in rabbits
    • Plopper CG, Weir AJ, Morin D, et al. Postnatal changes in the expression and distribution of pulmonary cytochrome P450 monooxygenases during Clara cell differentiation in rabbits. Mol. Pharmacol. 1993, 44:51-61.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 51-61
    • Plopper, C.G.1    Weir, A.J.2    Morin, D.3
  • 55
    • 0024539659 scopus 로고
    • Quantitation of mRNAs specific for the mixed-function oxidase system in rat liver and extrahepatic tissues during development
    • Simmons DL, Kasper CB Quantitation of mRNAs specific for the mixed-function oxidase system in rat liver and extrahepatic tissues during development. Arch. Biochem. Biophys. 1989, 271:10-20.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 10-20
    • Simmons, D.L.1    Kasper, C.B.2
  • 56
    • 0025439242 scopus 로고
    • The immunocytochemical detection of cytochrome P-450 monooxygenase in the lungs of fetal, neonatal, and adult hamsters
    • Strum JM, Ito T, Philpot RM, et al. The immunocytochemical detection of cytochrome P-450 monooxygenase in the lungs of fetal, neonatal, and adult hamsters. Am. J. Respir. Cell Mol. Biol. 1990, 2:493-501.
    • (1990) Am. J. Respir. Cell Mol. Biol. , vol.2 , pp. 493-501
    • Strum, J.M.1    Ito, T.2    Philpot, R.M.3
  • 57
    • 0020571548 scopus 로고
    • Developmental changes in rabbit pulmonary cytochrome P-450 subpopulations
    • Parandoosh Z, Franklin MR Developmental changes in rabbit pulmonary cytochrome P-450 subpopulations. Life Sci. 1983, 33:1255-1260.
    • (1983) Life Sci. , vol.33 , pp. 1255-1260
    • Parandoosh, Z.1    Franklin, M.R.2
  • 58
    • 0028816232 scopus 로고
    • Pulmonary cytochrome P-450 monooxygenase system and Clara cell differentiation in rats
    • Ji CM, Cardoso WV, Gebremichael A, et al. Pulmonary cytochrome P-450 monooxygenase system and Clara cell differentiation in rats. Am. J. Physiol. 1995, 269:L394-L402.
    • (1995) Am. J. Physiol. , vol.269 , pp. L394-L402
    • Ji, C.M.1    Cardoso, W.V.2    Gebremichael, A.3
  • 59
    • 0028504578 scopus 로고
    • Exposure to sidestream cigarette smoke alters bronchiolar epithelial cell differentiation in the postnatal rat lung
    • Ji CM, Plopper CG, Witschi HP, et al. Exposure to sidestream cigarette smoke alters bronchiolar epithelial cell differentiation in the postnatal rat lung. Am. J. Respir. Cell Mol. Biol. 1994, 11:312-320.
    • (1994) Am. J. Respir. Cell Mol. Biol. , vol.11 , pp. 312-320
    • Ji, C.M.1    Plopper, C.G.2    Witschi, H.P.3
  • 60
    • 0015435145 scopus 로고
    • Developmental aspects of hepatic and extrahepatic drug-metabolizing enzyme systems: microsomal enzymes and components in rabbit liver and lung during the first month of life
    • Fouts JR, Devereux TR Developmental aspects of hepatic and extrahepatic drug-metabolizing enzyme systems: microsomal enzymes and components in rabbit liver and lung during the first month of life. J. Pharmacol. Exp. Ther. 1972, 183:458-468.
    • (1972) J. Pharmacol. Exp. Ther. , vol.183 , pp. 458-468
    • Fouts, J.R.1    Devereux, T.R.2
  • 61
    • 0031226836 scopus 로고    scopus 로고
    • Pulmonary cytochrome P450 monooxygenase and Clara cell differentiation in mice
    • Fanucchi MV, Murphy ME, Buckpitt AR, et al. Pulmonary cytochrome P450 monooxygenase and Clara cell differentiation in mice. Am. J. Resp. Cell Molec. Biol. 1997, 17:302-314.
    • (1997) Am. J. Resp. Cell Molec. Biol. , vol.17 , pp. 302-314
    • Fanucchi, M.V.1    Murphy, M.E.2    Buckpitt, A.R.3
  • 62
    • 0027196605 scopus 로고
    • The postnatal development of drug-metabolizing enzymes in hepatic, pulmonary and renal tissues of the goat
    • Eltom SE, Babish JG, Schwark WS The postnatal development of drug-metabolizing enzymes in hepatic, pulmonary and renal tissues of the goat. J. Vet. Pharmacol. Ther. 1993, 16:152-163.
    • (1993) J. Vet. Pharmacol. Ther. , vol.16 , pp. 152-163
    • Eltom, S.E.1    Babish, J.G.2    Schwark, W.S.3
  • 63
    • 0032815163 scopus 로고    scopus 로고
    • CYP1A1 and CYP1B1, two hydrocarbon-inducible cytochromes P450 are constitutively expressed in neonate and adult goat liver, lung and kidney
    • Eltom SE, Schwark WS CYP1A1 and CYP1B1, two hydrocarbon-inducible cytochromes P450 are constitutively expressed in neonate and adult goat liver, lung and kidney. Pharmacol. Toxicol. 1999, 85:65-73.
    • (1999) Pharmacol. Toxicol. , vol.85 , pp. 65-73
    • Eltom, S.E.1    Schwark, W.S.2
  • 64
    • 0032610009 scopus 로고    scopus 로고
    • Flavin-containing monooxygenase isoform 2: developmental expression in fetal and neonatal rabbit lung
    • Larsen-Su S, Krueger SK, Yueh MF, et al. Flavin-containing monooxygenase isoform 2: developmental expression in fetal and neonatal rabbit lung. J. Biochem. Mol. Toxicol. 1999, 13:187-193.
    • (1999) J. Biochem. Mol. Toxicol. , vol.13 , pp. 187-193
    • Larsen-Su, S.1    Krueger, S.K.2    Yueh, M.F.3
  • 65
    • 0029621213 scopus 로고
    • Postnatal development of cytochrome P4501A1 and 2B1 in rat lung and liver: effect of aged and diluted sidestream cigarette smoke
    • Gebremichael A, Chang AM, Buckpitt AR, et al. Postnatal development of cytochrome P4501A1 and 2B1 in rat lung and liver: effect of aged and diluted sidestream cigarette smoke. Toxicol. Appl. Pharmacol. 1995, 135:246-253.
    • (1995) Toxicol. Appl. Pharmacol. , vol.135 , pp. 246-253
    • Gebremichael, A.1    Chang, A.M.2    Buckpitt, A.R.3
  • 66
    • 0033805156 scopus 로고    scopus 로고
    • Mammalian class theta GST and differential susceptibility to carcinogens: a review
    • Landi S Mammalian class theta GST and differential susceptibility to carcinogens: a review. Mutat. Res. 2000, 463:247-283.
    • (2000) Mutat. Res. , vol.463 , pp. 247-283
    • Landi, S.1
  • 68
    • 0024269217 scopus 로고
    • Glutathione transferases-structure and catalytic activity
    • Mannervik B, Danielson UH Glutathione transferases-structure and catalytic activity. Crc. Crit. Rev. Biochem. 1988, 23:283-337.
    • (1988) Crc. Crit. Rev. Biochem. , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 69
    • 0026546972 scopus 로고
    • Complementary DNA cloning, messenger RNA expression, and induction of alpha-class glutathione S-transferases in mouse tissues
    • Buetler TM, Eaton DL Complementary DNA cloning, messenger RNA expression, and induction of alpha-class glutathione S-transferases in mouse tissues. Cancer Res. 1992, 52:314-318.
    • (1992) Cancer Res. , vol.52 , pp. 314-318
    • Buetler, T.M.1    Eaton, D.L.2
  • 70
    • 0034329486 scopus 로고    scopus 로고
    • Development of phase II xenobiotic metabolizing enzymes in differentiating murine Clara cells
    • Fanucchi MV, Buckpitt AR, Murphy ME, et al. Development of phase II xenobiotic metabolizing enzymes in differentiating murine Clara cells. Toxicol. Appl. Pharmacol. 2000, 168:253-267.
    • (2000) Toxicol. Appl. Pharmacol. , vol.168 , pp. 253-267
    • Fanucchi, M.V.1    Buckpitt, A.R.2    Murphy, M.E.3
  • 71
    • 0017358843 scopus 로고
    • The perinatal development of epoxide-metabolizing enzyme activities in liver and extrahepatic organs of guinea pig and rabbit
    • James MO, Foureman GL, Law FC, et al. The perinatal development of epoxide-metabolizing enzyme activities in liver and extrahepatic organs of guinea pig and rabbit. Drug Metab. Dispos. 1977, 5:19-28.
    • (1977) Drug Metab. Dispos. , vol.5 , pp. 19-28
    • James, M.O.1    Foureman, G.L.2    Law, F.C.3
  • 72
    • 0025200365 scopus 로고
    • Human glutathione S-transferases: radioimmunoassay studies on the expression of alpha-, mu- and pi-class isoenzymes in developing lung and kidney
    • Beckett GJ, Howie AF, Hume R, et al. Human glutathione S-transferases: radioimmunoassay studies on the expression of alpha-, mu- and pi-class isoenzymes in developing lung and kidney. Biochim. Biophys. Acta 1990, 1036:176-182.
    • (1990) Biochim. Biophys. Acta , vol.1036 , pp. 176-182
    • Beckett, G.J.1    Howie, A.F.2    Hume, R.3
  • 73
    • 0025019298 scopus 로고
    • The alpha and pi isoenzymes of glutathione S-transferase in human fetal lung: in utero ontogeny compared with differentiation in lung organ culture
    • Cossar D, Bell J, Strange R, et al. The alpha and pi isoenzymes of glutathione S-transferase in human fetal lung: in utero ontogeny compared with differentiation in lung organ culture. Biochim. Biophys. Acta 1990, 1037:221-226.
    • (1990) Biochim. Biophys. Acta , vol.1037 , pp. 221-226
    • Cossar, D.1    Bell, J.2    Strange, R.3
  • 74
    • 0023868602 scopus 로고
    • Glutathione S-transferase in humans: development and tissue distribution
    • Pacifici GM, Franchi M, Colizzi C, et al. Glutathione S-transferase in humans: development and tissue distribution. Arch. Toxicol. 1988, 61:265-269.
    • (1988) Arch. Toxicol. , vol.61 , pp. 265-269
    • Pacifici, G.M.1    Franchi, M.2    Colizzi, C.3
  • 75
    • 0022509229 scopus 로고
    • The development of glutathione S-transferase and glutathione peroxidase activities in human lung
    • Fryer AA, Hume R, Strange RC The development of glutathione S-transferase and glutathione peroxidase activities in human lung. Biochim. Biophys. Acta 1986, 883:448-453.
    • (1986) Biochim. Biophys. Acta , vol.883 , pp. 448-453
    • Fryer, A.A.1    Hume, R.2    Strange, R.C.3
  • 76
    • 0028270676 scopus 로고
    • Glutathione S-transferase mediated detoxification and bioactivation of xenobiotics during early human pregnancy
    • Datta K, Roy SK, Mitra AK, et al. Glutathione S-transferase mediated detoxification and bioactivation of xenobiotics during early human pregnancy. Early Hum. Dev. 1994, 37:167-174.
    • (1994) Early Hum. Dev. , vol.37 , pp. 167-174
    • Datta, K.1    Roy, S.K.2    Mitra, A.K.3
  • 77
    • 0022371557 scopus 로고
    • The human glutathione S-transferases: developmental aspects of the GST1, GST2, and GST3 loci
    • Strange RC, Davis BA, Faulder CG, et al. The human glutathione S-transferases: developmental aspects of the GST1, GST2, and GST3 loci. Biochem. Genet. 1985, 23:1011-1028.
    • (1985) Biochem. Genet. , vol.23 , pp. 1011-1028
    • Strange, R.C.1    Davis, B.A.2    Faulder, C.G.3
  • 78
    • 0023762542 scopus 로고
    • Tissue distribution of drug-metabolizing enzymes in humans
    • Pacifici GM, Franchi M, Bencini C, et al. Tissue distribution of drug-metabolizing enzymes in humans. Xenobiotica 1988, 18:849-856.
    • (1988) Xenobiotica , vol.18 , pp. 849-856
    • Pacifici, G.M.1    Franchi, M.2    Bencini, C.3
  • 79
    • 0002802789 scopus 로고
    • Membrane-bound and soluble-fraction epoxide hydrolases: methodological aspects
    • Wiley, New York, D. Zakim, D.A. Vessey (Eds.)
    • Wixtrom RN, Hammock BD Membrane-bound and soluble-fraction epoxide hydrolases: methodological aspects. Biochemical Pharmacology and Toxicology 1985, 3-93. Wiley, New York. D. Zakim, D.A. Vessey (Eds.).
    • (1985) Biochemical Pharmacology and Toxicology , pp. 3-93
    • Wixtrom, R.N.1    Hammock, B.D.2
  • 80
    • 0024311510 scopus 로고
    • Rabbit microsomal epoxide hydrolase: isolation and characterization of the xenobiotic metabolizing enzyme cDNA
    • Hassett C, Turnblom SM, DeAngeles A, et al. Rabbit microsomal epoxide hydrolase: isolation and characterization of the xenobiotic metabolizing enzyme cDNA. Arch. Biochem. Biophys. 1989, 271:380-389.
    • (1989) Arch. Biochem. Biophys. , vol.271 , pp. 380-389
    • Hassett, C.1    Turnblom, S.M.2    DeAngeles, A.3
  • 81
    • 0025344378 scopus 로고
    • Cytochrome P 450 isoenzymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissues
    • de Waziers I, Cugnenc PH, Yang CS, et al. Cytochrome P 450 isoenzymes, epoxide hydrolase and glutathione transferases in rat and human hepatic and extrahepatic tissues. J. Pharmacol. Exp. Ther. 1990, 253:387-394.
    • (1990) J. Pharmacol. Exp. Ther. , vol.253 , pp. 387-394
    • de Waziers, I.1    Cugnenc, P.H.2    Yang, C.S.3
  • 82
    • 0023791757 scopus 로고
    • Organ distribution of epoxide hydrolases in cytosolic and microsomal fractions of normal and nafenopin-treated male DBA/2 mice
    • Waechter F, Bentley P, Bieri F, et al. Organ distribution of epoxide hydrolases in cytosolic and microsomal fractions of normal and nafenopin-treated male DBA/2 mice. Biochem. Pharmacol. 1988, 37:3897-3903.
    • (1988) Biochem. Pharmacol. , vol.37 , pp. 3897-3903
    • Waechter, F.1    Bentley, P.2    Bieri, F.3
  • 83
    • 0019942290 scopus 로고
    • Metabolism of styrene oxide in different human fetal tissues
    • Pacifici GM, Rane A Metabolism of styrene oxide in different human fetal tissues. Drug Metab. Dispos. 1982, 10:302-305.
    • (1982) Drug Metab. Dispos. , vol.10 , pp. 302-305
    • Pacifici, G.M.1    Rane, A.2
  • 84
    • 0023689586 scopus 로고
    • Cytosolic epoxide hydrolase in humans: development and tissue distribution
    • Pacifici GM, Temellini A, Giuliani L, et al. Cytosolic epoxide hydrolase in humans: development and tissue distribution. Arch. Toxicol. 1988, 62:254-257.
    • (1988) Arch. Toxicol. , vol.62 , pp. 254-257
    • Pacifici, G.M.1    Temellini, A.2    Giuliani, L.3
  • 85
    • 0028323534 scopus 로고
    • Developmental expression of human microsomal epoxide hydrolase
    • Omiecinski CJ, Aicher L, Swenson L Developmental expression of human microsomal epoxide hydrolase. J. Pharmacol. Exp. Ther. 1994, 269:417-423.
    • (1994) J. Pharmacol. Exp. Ther. , vol.269 , pp. 417-423
    • Omiecinski, C.J.1    Aicher, L.2    Swenson, L.3
  • 86
    • 0021272530 scopus 로고
    • Ontogeny of benzo(a)pyrene hydroxylase, epoxide hydrolase and glutathione-S transferase in the brain, lung and liver of C57B1/6 mice
    • Rouet P, Dansette P, Frayssinet C Ontogeny of benzo(a)pyrene hydroxylase, epoxide hydrolase and glutathione-S transferase in the brain, lung and liver of C57B1/6 mice. Dev. Pharmacol. Ther. 1984, 7:245-258.
    • (1984) Dev. Pharmacol. Ther. , vol.7 , pp. 245-258
    • Rouet, P.1    Dansette, P.2    Frayssinet, C.3
  • 87
    • 0023852210 scopus 로고
    • Regional distribution of xenobiotic metabolizing enzymes in respiratory airways of dogs
    • Bond JA, Harkema JR, Russell VI Regional distribution of xenobiotic metabolizing enzymes in respiratory airways of dogs. Drug Metab. Dispos. 1988, 16:116-124.
    • (1988) Drug Metab. Dispos. , vol.16 , pp. 116-124
    • Bond, J.A.1    Harkema, J.R.2    Russell, V.I.3
  • 88
    • 0019977274 scopus 로고
    • Ipomeanol 4-glucuronide, a major urinary metabolite of 4-ipomeanol in the rat
    • Statham CN, Dutcher JS, Kim SH, et al. Ipomeanol 4-glucuronide, a major urinary metabolite of 4-ipomeanol in the rat. Drug Metab. Dispos. 1982, 10:264-267.
    • (1982) Drug Metab. Dispos. , vol.10 , pp. 264-267
    • Statham, C.N.1    Dutcher, J.S.2    Kim, S.H.3
  • 89
    • 0025032790 scopus 로고
    • Localization, distribution, and induction of xenobiotic-metabolizing enzymes and aryl hydrocarbon hydroxylase activity within lung
    • Baron J, Voigt JM Localization, distribution, and induction of xenobiotic-metabolizing enzymes and aryl hydrocarbon hydroxylase activity within lung. Pharmacol. Ther. 1990, 47:419-445.
    • (1990) Pharmacol. Ther. , vol.47 , pp. 419-445
    • Baron, J.1    Voigt, J.M.2
  • 90
    • 0025204431 scopus 로고
    • Maturational development of drug-metabolizing enzymes in dogs
    • Kawalek JC, el Said KR Maturational development of drug-metabolizing enzymes in dogs. Am. J. Vet. Res. 1990, 51:1742-1745.
    • (1990) Am. J. Vet. Res. , vol.51 , pp. 1742-1745
    • Kawalek, J.C.1    el Said, K.R.2
  • 91
    • 0025204431 scopus 로고
    • Maturational development of drug-metabolizing enzymes in sheep
    • Kawalek JC, el Said KR Maturational development of drug-metabolizing enzymes in sheep. Am. J. Vet. Res. 1990, 51:1736-1741.
    • (1990) Am. J. Vet. Res. , vol.51 , pp. 1736-1741
    • Kawalek, J.C.1    el Said, K.R.2
  • 92
    • 0027478135 scopus 로고
    • Sulphation and glucuronidation of ritodrine in human foetal and adult tissues
    • Pacifici GM, Kubrich M, Giuliani L, et al. Sulphation and glucuronidation of ritodrine in human foetal and adult tissues. Eur. J. Clin. Pharmacol. 1993, 44:259-264.
    • (1993) Eur. J. Clin. Pharmacol. , vol.44 , pp. 259-264
    • Pacifici, G.M.1    Kubrich, M.2    Giuliani, L.3
  • 93
    • 0030047401 scopus 로고    scopus 로고
    • Differential expression and immunohistochemical localisation of the phenol and hydroxysteroid sulphotransferase enzyme families in the developing lung
    • Hume R, Barker EV, Coughtrie MW Differential expression and immunohistochemical localisation of the phenol and hydroxysteroid sulphotransferase enzyme families in the developing lung. Histochem. Cell Biol. 1996, 105:147-152.
    • (1996) Histochem. Cell Biol. , vol.105 , pp. 147-152
    • Hume, R.1    Barker, E.V.2    Coughtrie, M.W.3
  • 94
    • 0025316330 scopus 로고
    • Flavin-containing monooxygenases: enzymes adapted for multisubstrate specificity
    • Ziegler DM Flavin-containing monooxygenases: enzymes adapted for multisubstrate specificity. Trends Pharmacol. Sci. 1990, 11:321-324.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 321-324
    • Ziegler, D.M.1
  • 95
    • 0034280122 scopus 로고    scopus 로고
    • Human flavin-containing monooxygenase: substrate specificity and role in drug metabolism
    • Cashman JR Human flavin-containing monooxygenase: substrate specificity and role in drug metabolism. Curr. Drug Metab. 2000, 1:181-191.
    • (2000) Curr. Drug Metab. , vol.1 , pp. 181-191
    • Cashman, J.R.1
  • 96
    • 0030996250 scopus 로고    scopus 로고
    • Enzymology of human cytosolic sulfotransferases
    • Falany CN Enzymology of human cytosolic sulfotransferases. Faseb. J. 1997, 11:206-216.
    • (1997) Faseb. J. , vol.11 , pp. 206-216
    • Falany, C.N.1
  • 97
    • 0032549065 scopus 로고    scopus 로고
    • Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases
    • Coughtrie MW, Sharp S, Maxwell K, et al. Biology and function of the reversible sulfation pathway catalysed by human sulfotransferases and sulfatases. Chem. Biol. Interact. 1998, 109:3-27.
    • (1998) Chem. Biol. Interact. , vol.109 , pp. 3-27
    • Coughtrie, M.W.1    Sharp, S.2    Maxwell, K.3
  • 98
    • 0035479494 scopus 로고    scopus 로고
    • Human cytosolic sulphotransferases genetics, characteristics, toxicological aspects
    • Glatt H, Boeing H, Engelke CE, et al. Human cytosolic sulphotransferases genetics, characteristics, toxicological aspects. Mutat. Res. 2001, 482:27-40.
    • (2001) Mutat. Res. , vol.482 , pp. 27-40
    • Glatt, H.1    Boeing, H.2    Engelke, C.E.3
  • 99
    • 0034967098 scopus 로고    scopus 로고
    • Sulfation of thyroid hormone and dopamine during human development: ontogeny of phenol sulfotransferases and arylsulfatase in liver, lung, and brain
    • Richard K, Hume R, Kaptein E, et al. Sulfation of thyroid hormone and dopamine during human development: ontogeny of phenol sulfotransferases and arylsulfatase in liver, lung, and brain. J. Clin. Endocrinol. Metab. 2001, 86:2734-2742.
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 2734-2742
    • Richard, K.1    Hume, R.2    Kaptein, E.3
  • 100
    • 0002816074 scopus 로고    scopus 로고
    • Postnatal development and growth
    • Lippencott-Raven Publishers, Philadelphia, R.G. Crystal (Ed.)
    • Burri PH Postnatal development and growth. THE LUNG: Scientific Foundations 1997, 1013-1026. Lippencott-Raven Publishers, Philadelphia. Second Edition. R.G. Crystal (Ed.).
    • (1997) THE LUNG: Scientific Foundations , pp. 1013-1026
    • Burri, P.H.1
  • 101
    • 0019503120 scopus 로고
    • The development of the newborn rat lung in hyperoxia: a dose-response study of lung growth, maturation, and changes in antioxidant enzyme activities
    • Bucher JR, Roberts RJ The development of the newborn rat lung in hyperoxia: a dose-response study of lung growth, maturation, and changes in antioxidant enzyme activities. Pediatr. Res. 1981, 15:999-1008.
    • (1981) Pediatr. Res. , vol.15 , pp. 999-1008
    • Bucher, J.R.1    Roberts, R.J.2
  • 102
    • 0024205937 scopus 로고
    • Purification and biochemical characterization of the rabbit pulmonary glutathione S-transferase: stereoselectivity and activity toward pyrene 4,5-oxide
    • Serabjit-Singh CJ, Bend JR Purification and biochemical characterization of the rabbit pulmonary glutathione S-transferase: stereoselectivity and activity toward pyrene 4,5-oxide. Arch. Biochem. Biophys. 1988, 267:184-194.
    • (1988) Arch. Biochem. Biophys. , vol.267 , pp. 184-194
    • Serabjit-Singh, C.J.1    Bend, J.R.2
  • 103
    • 0025933684 scopus 로고
    • The major alpha-class glutathione S-transferases of rabbit lung and liver. Primary sequences, expression, and regulation
    • Gardlik S, Gasser R, Philpot RM, et al. The major alpha-class glutathione S-transferases of rabbit lung and liver. Primary sequences, expression, and regulation. J. Biol. Chem. 1991, 266:19681-19687.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19681-19687
    • Gardlik, S.1    Gasser, R.2    Philpot, R.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.