메뉴 건너뛰기




Volumn 279, Issue 19, 2012, Pages 3749-3761

Expression of human CYP27B1 in Escherichia coli and characterization in phospholipid vesicles

Author keywords

25 hydroxyvitamin D3; 25 hydroxyvitamin D3 1 hydroxylase; adrenodoxin; CYP27B1; phospholipid vesicles

Indexed keywords

25 HYDROXYERGOCALCIFEROL; ADRENODOXIN; CALCIDIOL 1 MONOOXYGENASE; CALCIFEDIOL; CARDIOLIPIN; CHAPERONIN; CHOLESTEROL MONOOXYGENASE (SIDE CHAIN CLEAVING); CYTOCHROME P450; CYTOCHROME P450 24A1; SECALCIFEROL; UNCLASSIFIED DRUG;

EID: 84866399293     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2012.08736.x     Document Type: Article
Times cited : (18)

References (60)
  • 1
    • 1642281100 scopus 로고    scopus 로고
    • Vitamin D: Importance in the prevention of cancers, type 1 diabetes, heart disease, and osteoporosis
    • Holick MF, (2004) Vitamin D: importance in the prevention of cancers, type 1 diabetes, heart disease, and osteoporosis. Am J Clin Nutr 79, 362-371. (Pubitemid 41115577)
    • (2004) American Journal of Clinical Nutrition , vol.79 , Issue.3 , pp. 362-371
    • Holick, M.F.1
  • 2
    • 8544284075 scopus 로고    scopus 로고
    • Enzymes involved in the activation and inactivation of vitamin D
    • DOI 10.1016/j.tibs.2004.10.005, PII S0968000404002701
    • Prosser DE, &, Jones G, (2004) Enzymes involved in the activation and inactivation of vitamin D. Trends Biochem Sci 29, 664-673. (Pubitemid 39491265)
    • (2004) Trends in Biochemical Sciences , vol.29 , Issue.12 , pp. 664-673
    • Prosser, D.E.1    Jones, G.2
  • 3
    • 78649447575 scopus 로고    scopus 로고
    • Cytochromes P450 are essential players in the vitamin D signaling system
    • Schuster I, (2011) Cytochromes P450 are essential players in the vitamin D signaling system. Biochim Biophys Acta 1814, 186-199.
    • (2011) Biochim Biophys Acta , vol.1814 , pp. 186-199
    • Schuster, I.1
  • 4
    • 0036307172 scopus 로고    scopus 로고
    • Vitamin D: The underappreciated D-lightful hormone that is important for skeletal and cellular health
    • DOI 10.1097/00060793-200202000-00011
    • Holick MF, (2002) Vitamin D: the underappreciated D-lightful hormone that is important for skeletal and cellular health. Curr Opin Endocrinol Diabetes Obes 9, 87-98. (Pubitemid 34747893)
    • (2002) Current Opinion in Endocrinology and Diabetes , vol.9 , Issue.1 , pp. 87-98
    • Holick, M.F.1
  • 5
    • 58149385796 scopus 로고    scopus 로고
    • Nonclassic actions of vitamin D
    • Bikle D, (2009) Nonclassic actions of vitamin D. J Clin Endocrinol Metab 94, 26-34.
    • (2009) J Clin Endocrinol Metab , vol.94 , pp. 26-34
    • Bikle, D.1
  • 9
    • 84861575206 scopus 로고    scopus 로고
    • Extrarenal expression of the 25-hydroxyvitamin D-1-hydroxylase
    • Adams JS, &, Hewison M, (2012) Extrarenal expression of the 25-hydroxyvitamin D-1-hydroxylase. Arch Biochem Biophys 523, 95-102.
    • (2012) Arch Biochem Biophys , vol.523 , pp. 95-102
    • Adams, J.S.1    Hewison, M.2
  • 10
    • 33750010974 scopus 로고    scopus 로고
    • Mitochondrial P450s
    • DOI 10.1016/j.cbi.2006.06.008, PII S0009279706001529
    • Omura T, (2006) Mitochondrial P450s. Chem Biol Interact 163, 86-93. (Pubitemid 44572220)
    • (2006) Chemico-Biological Interactions , vol.163 , Issue.1-2 , pp. 86-93
    • Omura, T.1
  • 11
  • 12
    • 0034130135 scopus 로고    scopus 로고
    • Human 25-hydroxyvitamin D-1α-hydroxylase: Cloning, mutations, and gene expression
    • Portale AA, &, Miller WL, (2000) Human 25-hydroxyvitamin D-1α-hydroxylase: cloning, mutations, and gene expression. Pediatr Nephrol 14, 620.
    • (2000) Pediatr Nephrol , vol.14 , pp. 620
    • Portale, A.A.1    Miller, W.L.2
  • 15
    • 48449097811 scopus 로고    scopus 로고
    • Kinetics of vitamin D3 metabolism by cytochrome P450scc (CYP11A1) in phospholipid vesicles and cyclodextrin
    • Tuckey RC, Nguyen MN, &, Slominski A, (2008) Kinetics of vitamin D3 metabolism by cytochrome P450scc (CYP11A1) in phospholipid vesicles and cyclodextrin. Int J Biochem Cell Biol 40, 2619-2626.
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 2619-2626
    • Tuckey, R.C.1    Nguyen, M.N.2    Slominski, A.3
  • 16
    • 84858284104 scopus 로고    scopus 로고
    • Metabolism of cholesterol, vitamin D3 and 20-hydroxyvitamin D3 incorporated into phospholipid vesicles by human CYP27A1
    • Tieu EW, Li W, Chen J, Baldisseri DM, Slominski AT, &, Tuckey RC, (2011) Metabolism of cholesterol, vitamin D3 and 20-hydroxyvitamin D3 incorporated into phospholipid vesicles by human CYP27A1. J Steroid Biochem Mol Biol 129, 163-171.
    • (2011) J Steroid Biochem Mol Biol , vol.129 , pp. 163-171
    • Tieu, E.W.1    Li, W.2    Chen, J.3    Baldisseri, D.M.4    Slominski, A.T.5    Tuckey, R.C.6
  • 17
    • 77950301126 scopus 로고    scopus 로고
    • Metabolism of substrates incorporated into phospholipid vesicles by mouse 25-hydroxyvitamin D3 1α-hydroxylase (CYP27B1)
    • Tang EKY, Voo KJQ, Nguyen MN, &, Tuckey RC, (2010) Metabolism of substrates incorporated into phospholipid vesicles by mouse 25-hydroxyvitamin D3 1α-hydroxylase (CYP27B1). J Steroid Biochem Mol Biol 119, 171-179.
    • (2010) J Steroid Biochem Mol Biol , vol.119 , pp. 171-179
    • Tang, E.K.Y.1    Voo, K.J.Q.2    Nguyen, M.N.3    Tuckey, R.C.4
  • 18
    • 0019320566 scopus 로고
    • Phospholipid vesicle-reconstituted cytochrome P-450scc. Mutually facilitated binding of cholesterol and adrenodoxin
    • Lambeth JD, Seybert DW, &, Kamin H, (1980) Phospholipid vesicle-reconstituted cytochrome P-450scc. Mutually facilitated binding of cholesterol and adrenodoxin. J Biol Chem 255, 138-143.
    • (1980) J Biol Chem , vol.255 , pp. 138-143
    • Lambeth, J.D.1    Seybert, D.W.2    Kamin, H.3
  • 19
    • 77955991921 scopus 로고    scopus 로고
    • Purified mouse CYP27B1 can hydroxylate 20,23-dihydroxyvitamin D3, producing 1α,20,23-trihydroxyvitamin D3, which has altered biological activity
    • Tang EKY, Li W, Janjetovic Z, Nguyen MN, Wang Z, Slominski A, &, Tuckey RC, (2010) Purified mouse CYP27B1 can hydroxylate 20,23-dihydroxyvitamin D3, producing 1α,20,23-trihydroxyvitamin D3, which has altered biological activity. Drug Metab Dispos 38, 1553-1559.
    • (2010) Drug Metab Dispos , vol.38 , pp. 1553-1559
    • Tang, E.K.Y.1    Li, W.2    Janjetovic, Z.3    Nguyen, M.N.4    Wang, Z.5    Slominski, A.6    Tuckey, R.C.7
  • 20
    • 0020645392 scopus 로고
    • Cytochrome P-450(scc)-phospholipid interactions: Evidence for a cardiolipin binding site and thermodynamics of enzyme interactions with cardiolipin, cholesterol, and adrenodoxin
    • Pember SO, Powell GL, &, Lambeth JD, (1983) Cytochrome P-450scc-phospholipid interactions. Evidence for a cardiolipin binding site and thermodynamics of enzyme interactions with cardiolipin, cholesterol, and adrenodoxin. J Biol Chem 258, 3198-3206. (Pubitemid 13130237)
    • (1983) Journal of Biological Chemistry , vol.258 , Issue.5 , pp. 3198-3206
    • Pember, S.O.1    Powell, G.L.2    Lambeth, J.D.3
  • 21
    • 0021985887 scopus 로고
    • Purification and analysis of phospholipids in the inner mitochondrial mmembrane fraction of bovine corpus luteum, and properties of cytochrome P-450(scc) incorporated into vesicles prepared from these phospholipids
    • DOI 10.1111/j.1432-1033.1985.tb08849.x
    • Tuckey RC, &, Stevenson PM, (1985) Purification and analysis of phospholipids in the inner mitochondrial membrane fraction of bovine corpus luteum, and properties of cytochrome P-450scc incorporated into vesicles prepared from these phospholipids. Eur J Biochem 148, 379-384. (Pubitemid 15093621)
    • (1985) European Journal of Biochemistry , vol.148 , Issue.2 , pp. 379-384
    • Tuckey, R.C.1    Stevenson, P.M.2
  • 22
  • 23
    • 0029990689 scopus 로고    scopus 로고
    • α-Branched 1,2-diacyl phosphatidylcholines as effectors of activity of cytochrome P450SCC (CYP11A1)
    • Schwarz D, Kisselev P, Wessel R, Jueptner O, &, Schmid RD, (1996) α-Branched 1,2-diacyl phosphatidylcholines as effectors of activity of cytochrome P450SCC (CYP11A1). J Biol Chem 271, 12840-12846.
    • (1996) J Biol Chem , vol.271 , pp. 12840-12846
    • Schwarz, D.1    Kisselev, P.2    Wessel, R.3    Jueptner, O.4    Schmid, R.D.5
  • 24
    • 0002819595 scopus 로고    scopus 로고
    • 3 1α-hydroxylase expressed in Escherichia coli
    • DOI 10.1046/j.1432-1327.1999.00096.x
    • Sakaki T, Sawada N, Takeyama K, Kato S, &, Inouye K, (1999) Enzymatic properties of mouse 25-hydroxyvitamin D3 1α-hydroxylase expressed in Escherichia coli. Eur J Biochem 259, 731-738. (Pubitemid 29075500)
    • (1999) European Journal of Biochemistry , vol.259 , Issue.3 , pp. 731-738
    • Sakaki, T.1    Sawada, N.2    Takeyama, K.-I.3    Kato, S.4    Inouye, K.5
  • 26
    • 0020490382 scopus 로고
    • Cytochrome P-450scc-substrate interactions. Studies of binding and catalytic activity using hydroxycholesterols
    • Lambeth JD, Kitchen SE, Farooqui AA, Tuckey R, &, Kamin H, (1982) Cytochrome P-450scc-substrate interactions. Studies of binding and catalytic activity using hydroxycholesterols. J Biol Chem 257, 1876-1884.
    • (1982) J Biol Chem , vol.257 , pp. 1876-1884
    • Lambeth, J.D.1    Kitchen, S.E.2    Farooqui, A.A.3    Tuckey, R.4    Kamin, H.5
  • 27
    • 0033559224 scopus 로고    scopus 로고
    • Enzymatic properties of vesicle-reconstituted human cytochrome P450scc (CYP11A1)
    • Kisselev P, Tuckey RC, Woods ST, Triantopoulos T, &, Schwarz D, (1999) Enzymatic properties of vesicle-reconstituted human cytochrome P450scc (CYP11A1). Eur J Biochem 260, 768-773.
    • (1999) Eur J Biochem , vol.260 , pp. 768-773
    • Kisselev, P.1    Tuckey, R.C.2    Woods, S.T.3    Triantopoulos, T.4    Schwarz, D.5
  • 28
    • 0019321486 scopus 로고
    • Phosphatidylcholine vesicle reconstituted cytochrome P-450scc. Role of the membrane in control of activity and spin state of the cytochrome
    • Lambeth JD, Kamin H, &, Seybert DW, (1980) Phosphatidylcholine vesicle reconstituted cytochrome P-450scc. Role of the membrane in control of activity and spin state of the cytochrome. J Biol Chem 255, 8282-8288.
    • (1980) J Biol Chem , vol.255 , pp. 8282-8288
    • Lambeth, J.D.1    Kamin, H.2    Seybert, D.W.3
  • 29
    • 0021249223 scopus 로고
    • Properties of bovine luteal cytochrome P-450(scc) incorporated into artificial phospholipid vesicles
    • DOI 10.1016/0020-711X(84)90166-6
    • scc incorporated into artificial phospholipid vesicles. Int J Biochem 16, 497-503. (Pubitemid 14100092)
    • (1984) International Journal of Biochemistry , vol.16 , Issue.5 , pp. 497-503
    • Tuckey, R.C.1    Stevenson, P.M.2
  • 30
    • 0019888070 scopus 로고
    • Cytochrome P-450scc. Cardiolipin as an effector of activity of a mitochondrial cytochrome P-450
    • Lambeth JD, (1981) Cytochrome P-450scc. Cardiolipin as an effector of activity of a mitochondrial cytochrome P-450. J Biol Chem 256, 4757-4762.
    • (1981) J Biol Chem , vol.256 , pp. 4757-4762
    • Lambeth, J.D.1
  • 31
    • 0031891483 scopus 로고    scopus 로고
    • Branched phosphatidylcholines stimulate activity of cytochrome P450SCC (CYP11A1) in phospholipid vesicles by enhancing cholesterol binding, membrane incorporation, and protein exchange
    • DOI 10.1074/jbc.273.3.1380
    • Kisselev P, Wessel R, Pisch S, Bornscheuer U, Schmid RD, &, Schwarz D, (1998) Branched phosphatidylcholines stimulate activity of cytochrome P450scc (CYP11A1) in phospholipid vesicles by enhancing cholesterol binding, membrane incorporation, and protein exchange. J Biol Chem 273, 1380-1386. (Pubitemid 28133656)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.3 , pp. 1380-1386
    • Kisselev, P.1    Wessel, R.2    Pisch, S.3    Bornscheuer, U.4    Schmid, R.-D.5    Schwarz, D.6
  • 33
    • 0019876871 scopus 로고
    • Adrenal mitochondrial cytochrome P-450scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover
    • Hanukoglu I, Spitsberg V, Bumpus JA, Dus KM, &, Jefcoate CR, (1981) Adrenal mitochondrial cytochrome P-450scc. Cholesterol and adrenodoxin interactions at equilibrium and during turnover. J Biol Chem 256, 4321-4328.
    • (1981) J Biol Chem , vol.256 , pp. 4321-4328
    • Hanukoglu, I.1    Spitsberg, V.2    Bumpus, J.A.3    Dus, K.M.4    Jefcoate, C.R.5
  • 34
    • 1542407809 scopus 로고    scopus 로고
    • Putative F-G loop is involved in association with the membrane in P450scc (P450 11A1)
    • DOI 10.1016/j.mce.2003.11.005, PII S0303720703005033
    • Pikuleva IA, (2004) Putative F-G loop is involved in association with the membrane in P450scc (P450 11A1). Mol Cell Endocrinol 215, 161-164. (Pubitemid 38333255)
    • (2004) Molecular and Cellular Endocrinology , vol.215 , Issue.1-2 , pp. 161-164
    • Pikuleva, I.A.1
  • 35
    • 57149125431 scopus 로고    scopus 로고
    • Studies of membrane topology of mitochondrial cholesterol hydroxylases CYPs 27A1 and 11A1
    • Pikuleva I, Mast N, Liao WL, &, Turko IV, (2008) Studies of membrane topology of mitochondrial cholesterol hydroxylases CYPs 27A1 and 11A1. Lipids 43, 1127-1132.
    • (2008) Lipids , vol.43 , pp. 1127-1132
    • Pikuleva, I.1    Mast, N.2    Liao, W.L.3    Turko, I.V.4
  • 36
    • 0020133397 scopus 로고
    • Stimulation of luteal mitochondrial cholesterol side-chain cleavage by cardiolipin
    • Tanaka T, &, Strauss JF, (1982) Stimulation of luteal mitochondrial cholesterol side-chain cleavage by cardiolipin. Endocrinology 110, 1592-1598.
    • (1982) Endocrinology , vol.110 , pp. 1592-1598
    • Tanaka, T.1    Strauss, J.F.2
  • 37
    • 0025195068 scopus 로고
    • 25-Hydroxyvitamin D3-1 alpha-hydroxylase in porcine hepatic tissue: Subcellular localization to both mitochondria and microsomes
    • Hollis BW, (1990) 25-Hydroxyvitamin D3-1 alpha-hydroxylase in porcine hepatic tissue: subcellular localization to both mitochondria and microsomes. Proc Natl Acad Sci USA 87, 6009-6013.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6009-6013
    • Hollis, B.W.1
  • 39
    • 0033565694 scopus 로고    scopus 로고
    • The concentration of adrenodoxin reductase limits cytochrome P450scc activity in the human placenta
    • DOI 10.1046/j.1432-1327.1999.00483.x
    • Tuckey RC, &, Sadleir J, (1999) The concentration of adrenodoxin reductase limits cytochrome P450scc activity in the human placenta. Eur J Biochem 263, 319-325. (Pubitemid 29337021)
    • (1999) European Journal of Biochemistry , vol.263 , Issue.2 , pp. 319-325
    • Tuckey, R.C.1    Sadleir, J.2
  • 40
    • 0021251061 scopus 로고
    • Properties of ferredoxin reductase and ferredoxin from the bovine corpus luteum
    • DOI 10.1016/0020-711X(84)90165-4
    • Tuckey RC, &, Stevenson PM, (1984) Properties of ferredoxin reductase and ferredoxin from the bovine corpus luteum. Int J Biochem 16, 489-495. (Pubitemid 14100091)
    • (1984) International Journal of Biochemistry , vol.16 , Issue.5 , pp. 489-495
    • Tuckey, R.C.1    Stevenson, P.M.2
  • 41
    • 0019320939 scopus 로고
    • scc. Mechanism of electron transport by adrenodoxin
    • scc. Mechanism of electron transport by adrenodoxin. J Biol Chem 255, 3057-3061.
    • (1980) J Biol Chem , vol.255 , pp. 3057-3061
    • Hanukoglu, I.1    Jefcoate, C.R.2
  • 42
    • 0027979002 scopus 로고
    • C-terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450
    • Uhlmann H, Kraft R, &, Bernhardt R, (1994) C-Terminal region of adrenodoxin affects its structural integrity and determines differences in its electron transfer function to cytochrome P-450. J Biol Chem 269, 22557-22564. (Pubitemid 24273360)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.36 , pp. 22557-22564
    • Uhlmann, H.1    Kraft, R.2    Bernhardt, R.3
  • 43
    • 0020755209 scopus 로고
    • Purification and characterization of renal ferredoxin from bovine renal mitochondria
    • Maruya N, Hiwatashi A, Ichikawa Y, &, Yamano T, (1983) Purification and characterization of renal ferredoxin from bovine renal mitochondria. J Biochem 93, 1239-1247.
    • (1983) J Biochem , vol.93 , pp. 1239-1247
    • Maruya, N.1    Hiwatashi, A.2    Ichikawa, Y.3    Yamano, T.4
  • 44
    • 0038468629 scopus 로고    scopus 로고
    • Human skin is a steroidogenic tissue: Steroidogenic enzymes and cofactors are expressed in epidermis, normal sebocytes, and an immortalized sebocyte cell line (SEB-1)
    • DOI 10.1046/j.1523-1747.2003.12244.x
    • Thiboutot D, Jabara S, McAllister JM, Sivarajah A, Gilliland K, Cong Z, &, Clawson G, (2003) Human skin is a steroidogenic tissue: steroidogenic enzymes and cofactors are expressed in epidermis, normal sebocytes, and an immortalized sebocyte cell line (SEB-1). J Invest Dermatol 120, 905-914. (Pubitemid 36702897)
    • (2003) Journal of Investigative Dermatology , vol.120 , Issue.6 , pp. 905-914
    • Thiboutot, D.1    Jabara, S.2    McAllister, J.M.3    Sivarajah, A.4    Gilliland, K.5    Cong, Z.6    Clawson, G.7
  • 45
    • 49449114001 scopus 로고    scopus 로고
    • Pharmacokinetics of vitamin D toxicity
    • Jones G, (2008) Pharmacokinetics of vitamin D toxicity. Am J Clin Nutr 88, 582S-586S.
    • (2008) Am J Clin Nutr , vol.88
    • Jones, G.1
  • 46
    • 82455167905 scopus 로고    scopus 로고
    • Vitamin D metabolism, cartilage and bone fracture repair
    • St-Arnaud R, &, Naja RP, (2011) Vitamin D metabolism, cartilage and bone fracture repair. Mol Cell Endocrinol 347, 48-54.
    • (2011) Mol Cell Endocrinol , vol.347 , pp. 48-54
    • St-Arnaud, R.1    Naja, R.P.2
  • 47
    • 35748952505 scopus 로고    scopus 로고
    • Self-assemblies of amphiphilic cyclodextrins
    • DOI 10.1007/s00249-007-0207-6
    • Roux M, Perly B, &, Djedaïni-Pilard F, (2007) Self-assemblies of amphiphilic cyclodextrins. Eur Biophys J 36, 861-867. (Pubitemid 350045050)
    • (2007) European Biophysics Journal , vol.36 , Issue.8 , pp. 861-867
    • Roux, M.1    Perly, B.2    Djedaini-Pilard, F.3
  • 48
    • 77449094112 scopus 로고    scopus 로고
    • Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism
    • Annalora AJ, Goodin DB, Hong WX, Zhang Q, Johnson EF, &, Stout CD, (2010) Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism. J Mol Biol 396, 441-451.
    • (2010) J Mol Biol , vol.396 , pp. 441-451
    • Annalora, A.J.1    Goodin, D.B.2    Hong, W.X.3    Zhang, Q.4    Johnson, E.F.5    Stout, C.D.6
  • 51
    • 33845681091 scopus 로고    scopus 로고
    • Proximal tubule endocytic apparatus as the specific renal uptake mechanism for vitamin D-binding protein/25-(OH)D3 complex
    • DOI 10.1111/j.1440-1797.2006.00704.x
    • Negri AL, (2006) Proximal tubule endocytic apparatus as the specific renal uptake mechanism for vitamin D-binding protein/25-(OH)D3 complex (Review Article). Nephrology 11, 510-515. (Pubitemid 44951232)
    • (2006) Nephrology , vol.11 , Issue.6 , pp. 510-515
    • Negri, A.L.1
  • 52
    • 0031830447 scopus 로고    scopus 로고
    • Expression of catalytically active human cytochrome P450scc in Escherichia coli and mutagenesis of isoleucine-462
    • DOI 10.1006/abbi.1998.0621
    • Woods ST, Sadleir J, Downs T, Triantopoulos T, Headlam MJ, &, Tuckey RC, (1998) Expression of catalytically active human cytochrome P450scc in Escherichia coli and mutagenesis of isoleucine-462. Arch Biochem Biophys 353, 109-115. (Pubitemid 28373035)
    • (1998) Archives of Biochemistry and Biophysics , vol.353 , Issue.1 , pp. 109-115
    • Woods, S.T.1    Sadleir, J.2    Downs, T.3    Triantopoulos, T.4    Headlam, M.J.5    Tuckey, R.C.6
  • 54
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 56
    • 0020490510 scopus 로고
    • Kinetics of the incorporation of adrenal cytochrome P-450scc into phosphatidylcholine vesicles
    • Tuckey RC, &, Kamin H, (1982) Kinetics of the incorporation of adrenal cytochrome P-450scc into phosphatidylcholine vesicles. J Biol Chem 257, 2887-2893.
    • (1982) J Biol Chem , vol.257 , pp. 2887-2893
    • Tuckey, R.C.1    Kamin, H.2
  • 57
    • 23844472962 scopus 로고    scopus 로고
    • The cytochrome P450scc system opens an alternate pathway of vitamin D3 metabolism
    • DOI 10.1111/j.1742-4658.2005.04819.x
    • Slominski A, Semak I, Zjawiony J, Wortsman J, Li W, Szczesniewski A, &, Tuckey RC, (2005) The cytochrome P450scc system opens an alternate pathway of vitamin D3 metabolism. FEBS J 272, 4080-4090. (Pubitemid 41160916)
    • (2005) FEBS Journal , vol.272 , Issue.16 , pp. 4080-4090
    • Slominski, A.1    Semak, I.2    Zjawiony, J.3    Wortsman, J.4    Li, W.5    Szczesniewski, A.6    Tuckey, R.C.7
  • 58
    • 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
  • 59
    • 0020482843 scopus 로고
    • Purification of cytochrome P-450D1α (25-hydroxyvitamin D3-1α-hydroxylase) of bovine kidney mitochondria
    • Hiwatashi A, Nishii Y, &, Ichikawa Y, (1982) Purification of cytochrome P-450D1α (25-hydroxyvitamin D3-1α-hydroxylase) of bovine kidney mitochondria. Biochem Biophys Res Commun 105, 320-327.
    • (1982) Biochem Biophys Res Commun , vol.105 , pp. 320-327
    • Hiwatashi, A.1    Nishii, Y.2    Ichikawa, Y.3
  • 60
    • 0015812892 scopus 로고
    • A new micromethod for determination of protein in cerebrospinal fluid and urine
    • Pesce MA, &, Strande CS, (1973) A new micromethod for determination of protein in cerebrospinal fluid and urine. Clin Chem 19, 1265-1267.
    • (1973) Clin Chem , vol.19 , pp. 1265-1267
    • Pesce, M.A.1    Strande, C.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.