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Volumn 144, Issue 1-3, 2000, Pages 211-219

Enhanced expression of CYP1B1 in Escherichia coli

Author keywords

Aminolevulinic acid; CYP1B1; Heme precursor; P450 heterologous expression

Indexed keywords

AMINOLEVULINIC ACID; CYTOCHROME P450 1B1; HEMOPROTEIN; UNCLASSIFIED DRUG;

EID: 0034599999     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-483X(99)00209-7     Document Type: Article
Times cited : (27)

References (24)
  • 1
    • 77049217262 scopus 로고
    • A new concept of development of anterior chamber angle: Its relationship to developmental glaucoma and other structural anomalies
    • Allen L., Burion H.M., Braley A.E. A new concept of development of anterior chamber angle: its relationship to developmental glaucoma and other structural anomalies. Arch. Ophthalmol. 53:1955;783-798.
    • (1955) Arch. Ophthalmol. , vol.53 , pp. 783-798
    • Allen, L.1    Burion, H.M.2    Braley, A.E.3
  • 2
    • 0019742616 scopus 로고
    • The development of the trabecular meshwork and its abnormality in primary infantile glaucoma
    • Anderson D.R. The development of the trabecular meshwork and its abnormality in primary infantile glaucoma. Trans. Am. Ophthalmol. Soc. 79:1981;458-485.
    • (1981) Trans. Am. Ophthalmol. Soc. , vol.79 , pp. 458-485
    • Anderson, D.R.1
  • 3
    • 0002001058 scopus 로고
    • Pathogenesis of congenital glaucoma
    • Barkan O. Pathogenesis of congenital glaucoma. Am. J. Ophthalmol. 40:1955;1-11.
    • (1955) Am. J. Ophthalmol. , vol.40 , pp. 1-11
    • Barkan, O.1
  • 4
    • 0016170054 scopus 로고
    • Maximal exponential growth rate and yield of E. coli obtainable in a bench-scale fermentor
    • Bauer S., Shiloach J. Maximal exponential growth rate and yield of E. coli obtainable in a bench-scale fermentor. Biotechnol. Bioeng. 16:1974;933-941.
    • (1974) Biotechnol. Bioeng. , vol.16 , pp. 933-941
    • Bauer, S.1    Shiloach, J.2
  • 5
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt D.S., Hwang P.M., Glatt C.E., Lowenstein C., Reed R.R., Snyder S.H. Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature. 351:1991;714-718.
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5    Snyder, S.H.6
  • 6
    • 0028826889 scopus 로고
    • Cytochrome CYP1A1 and CYP1B1 in the rat mammary gland: Cell-specific expression and regulation by polycyclic aromatic hydrocarbons and hormones
    • Christou M., Savas U., Schroeder S., Shen X., Thompson T., Gould M.N., Jefcoate C.R. Cytochrome CYP1A1 and CYP1B1 in the rat mammary gland: cell-specific expression and regulation by polycyclic aromatic hydrocarbons and hormones. Mol. Cell. Endocrinol. 115:1995;41-50.
    • (1995) Mol. Cell. Endocrinol. , vol.115 , pp. 41-50
    • Christou, M.1    Savas, U.2    Schroeder, S.3    Shen, X.4    Thompson, T.5    Gould, M.N.6    Jefcoate, C.R.7
  • 8
    • 0026485793 scopus 로고
    • High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase flavoprotein
    • Fisher C.W., Shet M.S., Caudle D.L., Martin-Wixtrom C.A., Estabrook R.W. High-level expression in Escherichia coli of enzymatically active fusion proteins containing the domains of mammalian cytochromes P450 and NADPH-P450 reductase flavoprotein. Proc. Natl. Acad. Sci. USA. 89:1992;10817-10821.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10817-10821
    • Fisher, C.W.1    Shet, M.S.2    Caudle, D.L.3    Martin-Wixtrom, C.A.4    Estabrook, R.W.5
  • 9
    • 0028977906 scopus 로고
    • Expression of cytochrome P450 2D6 in Escherichia coli: Purification, and spectral and catalytic characterization
    • Gillam E.M.K., Guo Z., Martin M.V., Jenkins C.M.J., Guengerich F.P. Expression of cytochrome P450 2D6 in Escherichia coli: purification, and spectral and catalytic characterization. Arch. Biochem. Biophys. 319:1995;540-550.
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 540-550
    • Gillam, E.M.K.1    Guo, Z.2    Martin, M.V.3    Jenkins, C.M.J.4    Guengerich, F.P.5
  • 11
    • 0018293514 scopus 로고
    • Observations on the development of the anterior chamber angle with reference to the pathogenesis of congenital glaucoma
    • Kupfer C., Kaiser-Kupfer M. Observations on the development of the anterior chamber angle with reference to the pathogenesis of congenital glaucoma. Am. J. Ophthalmol. 88:1979;423-426.
    • (1979) Am. J. Ophthalmol. , vol.88 , pp. 423-426
    • Kupfer, C.1    Kaiser-Kupfer, M.2
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0026376260 scopus 로고
    • Proposed role of drug-metabolizing enzymes: Regulation of steady state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions
    • Nebert D. Proposed role of drug-metabolizing enzymes: regulation of steady state levels of the ligands that effect growth, homeostasis, differentiation, and neuroendocrine functions. Mol. Endocrinol. 5:1991;1203-1214.
    • (1991) Mol. Endocrinol. , vol.5 , pp. 1203-1214
    • Nebert, D.1
  • 14
    • 0026502760 scopus 로고
    • Primary structure of human thromboxane synthase determined from the cDNA sequence
    • Ohashi K., Ruan K., Kulmacz R., Wu K., Wang L. Primary structure of human thromboxane synthase determined from the cDNA sequence. J. Biol. Chem. 267:1992;789-793.
    • (1992) J. Biol. Chem. , vol.267 , pp. 789-793
    • Ohashi, K.1    Ruan, K.2    Kulmacz, R.3    Wu, K.4    Wang, L.5
  • 15
    • 50449100139 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties
    • Omura T., Sato R. The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem. 239:1964;2379-2385.
    • (1964) J. Biol. Chem. , vol.239 , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 17
    • 0028358220 scopus 로고
    • Expression of modified human cytochrome P450 1A2 in Escherichia coli: Stabilization, purification, spectral characterization, and catalytic activities of the enzyme
    • Sandhu P., Guo Z., Baba T., Martin M., Tukey R., Guengerich F. Expression of modified human cytochrome P450 1A2 in Escherichia coli: stabilization, purification, spectral characterization, and catalytic activities of the enzyme. Arch. Biochem. Biophys. 309:1994;168-177.
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 168-177
    • Sandhu, P.1    Guo, Z.2    Baba, T.3    Martin, M.4    Tukey, R.5    Guengerich, F.6
  • 20
    • 0002225779 scopus 로고    scopus 로고
    • The fate of xenobiotics in the body
    • E. Arinç, J.B. Schenkman, Hodgson E. New York: Plenum. Nato ASI Series A: Life Sciences
    • Schenkman J.B. The fate of xenobiotics in the body. Arinç E., Schenkman J.B., Hodgson E. Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes. 303:1999;1-20 Plenum, New York. Nato ASI Series A: Life Sciences.
    • (1999) Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes , vol.303 , pp. 1-20
    • Schenkman, J.B.1
  • 21
    • 0642345971 scopus 로고    scopus 로고
    • Spectral analysis of cytochrome P450
    • I.R. Phillips, & E.A. Shephard. Cytochrome P450 Protocols. Totowa, NJ: Humana Press
    • Schenkman J.B., Jansson I. Spectral analysis of cytochrome P450. Phillips I.R., Shephard E.A. Cytochrome P450 Protocols. Methods in Molecular Biology. 107:1998;25-33 Humana Press, Totowa, NJ.
    • (1998) Methods in Molecular Biology , vol.107 , pp. 25-33
    • Schenkman, J.B.1    Jansson, I.2
  • 23
    • 0030942553 scopus 로고    scopus 로고
    • Identification of three different truncating mutations in cytochrome P4501B1 (CYP1B1) as the principal cause of primary congenital glaucoma (buphthalmos) in families linked to the GLC3A locus on chromosome 2p21
    • Stoilov I., Akarsu A.N., Sarfarazi M. Identification of three different truncating mutations in cytochrome P4501B1 (CYP1B1) as the principal cause of primary congenital glaucoma (buphthalmos) in families linked to the GLC3A locus on chromosome 2p21. Hum. Mol. Genet. 6:1997;641-647.
    • (1997) Hum. Mol. Genet. , vol.6 , pp. 641-647
    • Stoilov, I.1    Akarsu, A.N.2    Sarfarazi, M.3
  • 24
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.