메뉴 건너뛰기




Volumn 22, Issue 7, 2013, Pages 964-979

Functional studies of N-terminally modified CYP2J2 epoxygenase in model lipid bilayers

Author keywords

CYP epoxygenases; CYP2J2; Cytochrome P450; Cytochrome P450 reductase; Ebastine hydroxylation; Eicosanoids; Lipid bilayers; N terminus modifications; Nanodiscs; Protein expression; Protein purification

Indexed keywords

CYTOCHROME P450 2J2; CYTOCHROME P450 REDUCTASE; EBASTINE; NANODISC; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE;

EID: 84881308967     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.2280     Document Type: Article
Times cited : (39)

References (76)
  • 1
    • 84861120187 scopus 로고    scopus 로고
    • Role of basic science in the development of new medicines: Examples from the eicosanoid field
    • Samuelsson B (2012) Role of basic science in the development of new medicines: examples from the eicosanoid field. J Biol Chem 287:10070-10080.
    • (2012) J Biol Chem , vol.287 , pp. 10070-10080
    • Samuelsson, B.1
  • 2
    • 33846473252 scopus 로고    scopus 로고
    • Cytochrome P450 systems-biological variations of electron transport chains
    • Hannemann F, Bichet A, Ewen KM, Bernhardt R (2007) Cytochrome P450 systems-biological variations of electron transport chains. Biochim Biophys Acta 1770:330-344.
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 330-344
    • Hannemann, F.1    Bichet, A.2    Ewen, K.M.3    Bernhardt, R.4
  • 3
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • Bernhardt R (2006) Cytochromes P450 as versatile biocatalysts. J Biotechnol 124:128-145.
    • (2006) J Biotechnol , vol.124 , pp. 128-145
    • Bernhardt, R.1
  • 5
    • 81155155630 scopus 로고    scopus 로고
    • CYP-eicosanoids-A new link between omega-3 fatty acids and cardiac disease?
    • Westphal C, Konkel A, Schunck WH (2011) CYP-eicosanoids-a new link between omega-3 fatty acids and cardiac disease? Prostaglandins Other Lipid Mediat 96: 99-108.
    • (2011) Prostaglandins Other Lipid Mediat , vol.96 , pp. 99-108
    • Westphal, C.1    Konkel, A.2    Schunck, W.H.3
  • 7
    • 77956252084 scopus 로고    scopus 로고
    • Overexpression of cytochrome P450 epoxygenases prevents development of hypertension in spontaneously hypertensive rats by enhancing atrial natriuretic peptide
    • Xiao B, Li X, Yan J, Yu X, Yang G, Xiao X, Voltz JW, Zeldin DC, Wang DW (2010) Overexpression of cytochrome P450 epoxygenases prevents development of hypertension in spontaneously hypertensive rats by enhancing atrial natriuretic peptide. J Pharmacol Exp Ther 334:784-794.
    • (2010) J Pharmacol Exp Ther , vol.334 , pp. 784-794
    • Xiao, B.1    Li, X.2    Yan, J.3    Yu, X.4    Yang, G.5    Xiao, X.6    Voltz, J.W.7    Zeldin, D.C.8    Wang, D.W.9
  • 8
    • 84856747668 scopus 로고    scopus 로고
    • Epoxides and soluble epoxide hydrolase in cardiovascular physiology
    • Imig JD (2012) Epoxides and soluble epoxide hydrolase in cardiovascular physiology. Physiol Rev 92:101-130.
    • (2012) Physiol Rev , vol.92 , pp. 101-130
    • Imig, J.D.1
  • 9
    • 70349636047 scopus 로고    scopus 로고
    • Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases
    • Imig JD, Hammock BD (2009) Soluble epoxide hydrolase as a therapeutic target for cardiovascular diseases. Nat Rev Drug Discov 8:794-805.
    • (2009) Nat Rev Drug Discov , vol.8 , pp. 794-805
    • Imig, J.D.1    Hammock, B.D.2
  • 19
    • 0036842039 scopus 로고    scopus 로고
    • Involvement of CYP2J2 on the intestinal first-pass metabolism of antihistamine drug, astemizole
    • Matsumoto S, Hirama T, Matsubara T, Nagata K, Yamazoe Y (2002) Involvement of CYP2J2 on the intestinal first-pass metabolism of antihistamine drug, astemizole. Drug Metab Dispos 30:1240-1245.
    • (2002) Drug Metab Dispos , vol.30 , pp. 1240-1245
    • Matsumoto, S.1    Hirama, T.2    Matsubara, T.3    Nagata, K.4    Yamazoe, Y.5
  • 20
    • 0642315074 scopus 로고    scopus 로고
    • Signals for retention of cytochrome P450 in the endoplasmic reticulum
    • Skorupa E, Kemper B (1998) Signals for retention of cytochrome P450 in the endoplasmic reticulum. Methods Mol Biol 107:251-266.
    • (1998) Methods Mol Biol , vol.107 , pp. 251-266
    • Skorupa, E.1    Kemper, B.2
  • 21
    • 0036028821 scopus 로고    scopus 로고
    • Analyzing binding of Nterminal truncated, microsomal cytochrome P450s to membranes
    • Cosme J, Johnson EF (2002) Analyzing binding of Nterminal truncated, microsomal cytochrome P450s to membranes. Methods Enzymol 357:116-120.
    • (2002) Methods Enzymol , vol.357 , pp. 116-120
    • Cosme, J.1    Johnson, E.F.2
  • 22
    • 0034738973 scopus 로고    scopus 로고
    • Microsomal cytochrome P450 2C5: Comparison to microbial P450s and unique features
    • Williams PA, Cosme J, Sridhar V, Johnson EF, McRee DE (2000) Microsomal cytochrome P450 2C5: comparison to microbial P450s and unique features. J Inorg Biochem 81:183-190.
    • (2000) J Inorg Biochem , vol.81 , pp. 183-190
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 23
    • 0038690559 scopus 로고    scopus 로고
    • Protein engineering of thromboxane synthase: Conversion of membrane-bound to soluble form
    • Hsu PY, Wang LH (2003) Protein engineering of thromboxane synthase: conversion of membrane-bound to soluble form. Arch Biochem Biophys 416:38-46.
    • (2003) Arch Biochem Biophys , vol.416 , pp. 38-46
    • Hsu, P.Y.1    Wang, L.H.2
  • 25
    • 0031106366 scopus 로고    scopus 로고
    • Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus
    • von Wachenfeldt C, Richardson TH, Cosme J, Johnson EF (1997) Microsomal P450 2C3 is expressed as a soluble dimer in Escherichia coli following modification of its N-terminus. Arch Biochem Biophys 339:107-114.
    • (1997) Arch Biochem Biophys , vol.339 , pp. 107-114
    • Von Wachenfeldt, C.1    Richardson, T.H.2    Cosme, J.3    Johnson, E.F.4
  • 26
    • 34147188077 scopus 로고    scopus 로고
    • Effects of N-terminal modification of recombinant human cytochrome P450 1A2 on catalytic activity
    • Kim HJ, Lee SB, Guengerich FP, Park YI, Dong MS (2007) Effects of N-terminal modification of recombinant human cytochrome P450 1A2 on catalytic activity. Xenobiotica 37:356-365.
    • (2007) Xenobiotica , vol.37 , pp. 356-365
    • Kim, H.J.1    Lee, S.B.2    Guengerich, F.P.3    Park, Y.I.4    Dong, M.S.5
  • 27
    • 80054709526 scopus 로고    scopus 로고
    • Membrane position of ibuprofen agrees with suggested access path entrance to cytochrome P450 2C9 active site
    • Berka K, Hendrychova T, Anzenbacher P, Otyepka M (2011) Membrane position of ibuprofen agrees with suggested access path entrance to cytochrome P450 2C9 active site. J Phys Chem A 115:11248-11255.
    • (2011) J Phys Chem A , vol.115 , pp. 11248-11255
    • Berka, K.1    Hendrychova, T.2    Anzenbacher, P.3    Otyepka, M.4
  • 30
    • 77951903021 scopus 로고    scopus 로고
    • Membrane protein assembly into Nanodiscs
    • Bayburt TH, Sligar SG (2010) Membrane protein assembly into Nanodiscs. FEBS Lett 584:1721-1727.
    • (2010) FEBS Lett , vol.584 , pp. 1721-1727
    • Bayburt, T.H.1    Sligar, S.G.2
  • 32
    • 33745511381 scopus 로고    scopus 로고
    • Functional reconstitution of Beta2-adrenergic receptors utilizing self-assembling Nanodisc technology
    • Leitz AJ, Bayburt TH, Barnakov AN, Springer BA, Sligar SG (2006) Functional reconstitution of Beta2-adrenergic receptors utilizing self-assembling Nanodisc technology. Biotechniques 40:601-612.
    • (2006) Biotechniques , vol.40 , pp. 601-612
    • Leitz, A.J.1    Bayburt, T.H.2    Barnakov, A.N.3    Springer, B.A.4    Sligar, S.G.5
  • 33
    • 33746856934 scopus 로고    scopus 로고
    • Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties
    • Boldog T, Grimme S, Li M, Sligar SG, Hazelbauer GL (2006) Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties. Proc Natl Acad Sci USA 103:11509-11514.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11509-11514
    • Boldog, T.1    Grimme, S.2    Li, M.3    Sligar, S.G.4    Hazelbauer, G.L.5
  • 34
    • 33847639732 scopus 로고    scopus 로고
    • Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins
    • Nath A, Atkins WM, Sligar SG (2007) Applications of phospholipid bilayer nanodiscs in the study of membranes and membrane proteins. Biochemistry 46:2059-2069.
    • (2007) Biochemistry , vol.46 , pp. 2059-2069
    • Nath, A.1    Atkins, W.M.2    Sligar, S.G.3
  • 35
    • 36148934091 scopus 로고    scopus 로고
    • Redox potential control by drug binding to cytochrome P450 3A4
    • Das A, Grinkova YV, Sligar SG (2007) Redox potential control by drug binding to cytochrome P450 3A4. J Am Chem Soc 129:13778-13779.
    • (2007) J Am Chem Soc , vol.129 , pp. 13778-13779
    • Das, A.1    Grinkova, Y.V.2    Sligar, S.G.3
  • 36
    • 73149090794 scopus 로고    scopus 로고
    • Modulation of the cytochrome P450 reductase redox potential by the phospholipid bilayer
    • Das A, Sligar SG (2009) Modulation of the cytochrome P450 reductase redox potential by the phospholipid bilayer. Biochemistry 48:12104-12112.
    • (2009) Biochemistry , vol.48 , pp. 12104-12112
    • Das, A.1    Sligar, S.G.2
  • 37
    • 77958613305 scopus 로고    scopus 로고
    • Nanomechanical detection of cholera toxin using microcantilevers functionalized with ganglioside nanodiscs
    • Tark SH, Das A, Sligar S, Dravid VP (2010) Nanomechanical detection of cholera toxin using microcantilevers functionalized with ganglioside nanodiscs. Nanotechnology 21:435502.
    • (2010) Nanotechnology , vol.21 , pp. 435502
    • Tark, S.H.1    Das, A.2    Sligar, S.3    Dravid, V.P.4
  • 38
    • 84856228232 scopus 로고    scopus 로고
    • Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs
    • Marty MT, Das A, Sligar SG (2012) Ultra-thin layer MALDI mass spectrometry of membrane proteins in nanodiscs. Anal Bioanal Chem 402:721-729.
    • (2012) Anal Bioanal Chem , vol.402 , pp. 721-729
    • Marty, M.T.1    Das, A.2    Sligar, S.G.3
  • 39
    • 66149100484 scopus 로고    scopus 로고
    • Screening of type i and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy
    • Das A, Zhao J, Schatz GC, Sligar SG, Van Duyne RP (2009) Screening of type I and II drug binding to human cytochrome P450-3A4 in nanodiscs by localized surface plasmon resonance spectroscopy. Anal Chem 81:3754-3759.
    • (2009) Anal Chem , vol.81 , pp. 3754-3759
    • Das, A.1    Zhao, J.2    Schatz, G.C.3    Sligar, S.G.4    Van Duyne, R.P.5
  • 40
    • 33748029518 scopus 로고    scopus 로고
    • Resonance surface plasmon spectroscopy: Low molecular weight substrate binding to cytochrome p450
    • Zhao J, Das A, Zhang X, Schatz GC, Sligar SG, Van Duyne RP (2006) Resonance surface plasmon spectroscopy: low molecular weight substrate binding to cytochrome p450. J Am Chem Soc 128:11004-11005.
    • (2006) J Am Chem Soc , vol.128 , pp. 11004-11005
    • Zhao, J.1    Das, A.2    Zhang, X.3    Schatz, G.C.4    Sligar, S.G.5    Van Duyne, R.P.6
  • 41
    • 37349017983 scopus 로고    scopus 로고
    • Heterologous expression and characterization of wild-type human cytochrome P450 1A2 without conventional N-terminal modification in Escherichia coli
    • Kim DH, Kim KH, Isin EM, Guengerich FP, Chae HZ, Ahn T, Yun CH (2008) Heterologous expression and characterization of wild-type human cytochrome P450 1A2 without conventional N-terminal modification in Escherichia coli. Protein Expr Purif 57:188-200.
    • (2008) Protein Expr Purif , vol.57 , pp. 188-200
    • Kim, D.H.1    Kim, K.H.2    Isin, E.M.3    Guengerich, F.P.4    Chae, H.Z.5    Ahn, T.6    Yun, C.H.7
  • 43
    • 0023395492 scopus 로고
    • Influence of the codon following the aug initiation codon on the expression of a modified Lacz gene in Escherichia coli
    • Looman AC, Bodlaender J, Comstock LJ, Eaton D, Jhurani P, Deboer HA, Vanknippenberg PH (1987) Influence of the codon following the aug initiation codon on the expression of a modified Lacz gene in Escherichia coli. EMBO J 6:2489-2492.
    • (1987) EMBO J , vol.6 , pp. 2489-2492
    • Looman, A.C.1    Bodlaender, J.2    Comstock, L.J.3    Eaton, D.4    Jhurani, P.5    Deboer, H.A.6    Vanknippenberg, P.H.7
  • 44
    • 0025994649 scopus 로고
    • Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli
    • Barnes HJ, Arlotto MP, Waterman MR (1991) Expression and enzymatic activity of recombinant cytochrome P450 17 alpha-hydroxylase in Escherichia coli. Proc Natl Acad Sci USA 88:5597-5601.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5597-5601
    • Barnes, H.J.1    Arlotto, M.P.2    Waterman, M.R.3
  • 46
    • 0024344770 scopus 로고
    • The role of bases upstream of the Shine-Dalgarno region and in the coding sequence in the control of gene expression in Escherichia coli: Translation and stability of mRNAs in vivo
    • Schauder B, McCarthy JE (1989) The role of bases upstream of the Shine-Dalgarno region and in the coding sequence in the control of gene expression in Escherichia coli: translation and stability of mRNAs in vivo. Gene 78:59-72.
    • (1989) Gene , vol.78 , pp. 59-72
    • Schauder, B.1    McCarthy, J.E.2
  • 47
    • 2542433007 scopus 로고    scopus 로고
    • Identification of a novel rat microsomal vitamin D3 25-hydroxylase
    • Yamasaki T, Izumi S, Ide H, Ohyama Y (2004) Identification of a novel rat microsomal vitamin D3 25-hydroxylase. J Biol Chem 279:22848-22856.
    • (2004) J Biol Chem , vol.279 , pp. 22848-22856
    • Yamasaki, T.1    Izumi, S.2    Ide, H.3    Ohyama, Y.4
  • 48
    • 84856477784 scopus 로고    scopus 로고
    • Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001
    • DeVore NM, Scott E (2012) Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001. Nature 482:116-119.
    • (2012) Nature , vol.482 , pp. 116-119
    • Devore, N.M.1    Scott, E.2
  • 51
    • 0032464019 scopus 로고    scopus 로고
    • GroEL/GroES: Structure and function of a two-stroke folding machine
    • Xu Z, Sigler P (1998) GroEL/GroES: structure and function of a two-stroke folding machine. J Struct Biol 124:129-141.
    • (1998) J Struct Biol , vol.124 , pp. 129-141
    • Xu, Z.1    Sigler, P.2
  • 53
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar SG (1976) Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 15:5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 54
    • 34147112191 scopus 로고    scopus 로고
    • Cooperativity in cytochrome P450 3A4: Linkages in substrate binding, spin state, uncoupling, and product formation
    • Denisov IG, Baas BJ, Grinkova YV, Sligar SG (2007) Cooperativity in cytochrome P450 3A4: linkages in substrate binding, spin state, uncoupling, and product formation. J Biol Chem 282:7066-7076.
    • (2007) J Biol Chem , vol.282 , pp. 7066-7076
    • Denisov, I.G.1    Baas, B.J.2    Grinkova, Y.V.3    Sligar, S.G.4
  • 56
    • 47749092044 scopus 로고    scopus 로고
    • Determinants of cytochrome P450 2C8 substrate binding: Structures of complexes with montelukast, troglitazone, felodipine, and 9-cisretinoic acid
    • Schoch GA, Yano JK, Sansen S, Dansette PM, Stout CD, Johnson EF (2008) Determinants of cytochrome P450 2C8 substrate binding: structures of complexes with montelukast, troglitazone, felodipine, and 9-cisretinoic acid. J Biol Chem 283:17227-17237.
    • (2008) J Biol Chem , vol.283 , pp. 17227-17237
    • Schoch, G.A.1    Yano, J.K.2    Sansen, S.3    Dansette, P.M.4    Stout, C.D.5    Johnson, E.F.6
  • 59
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the Web: A case study using the Phyre server
    • Kelley LA, Sternberg M (2009) Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4:363-371.
    • (2009) Nat Protoc , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.2
  • 61
    • 8844229574 scopus 로고    scopus 로고
    • Simultaneous determination of ebastine and its three metabolites in plasma using liquid chromatography-tandem mass spectrometry
    • Kang W, Liu KH, Ryu JY, Shin J (2004) Simultaneous determination of ebastine and its three metabolites in plasma using liquid chromatography-tandem mass spectrometry. J Chromatogr B Analyt Technol Biomed Life Sci 813:75-80.
    • (2004) J Chromatogr B Analyt Technol Biomed Life Sci , vol.813 , pp. 75-80
    • Kang, W.1    Liu, K.H.2    Ryu, J.Y.3    Shin, J.4
  • 62
    • 33751112296 scopus 로고    scopus 로고
    • Characterization of ebastine, hydroxyebastine, and carebastine metabolism by human liver microsomes and expressed cytochrome P450 enzymes: Major roles for CYP2J2 and CYP3A
    • Liu KH, Kim MG, Lee DJ, Yoon YJ, Kim MJ, Shon JH, Choi CS, Choi YK, Desta Z, Shin JG (2006) Characterization of ebastine, hydroxyebastine, and carebastine metabolism by human liver microsomes and expressed cytochrome P450 enzymes: major roles for CYP2J2 and CYP3A. Drug Metab Dispos 34:1793-1797.
    • (2006) Drug Metab Dispos , vol.34 , pp. 1793-1797
    • Liu, K.H.1    Kim, M.G.2    Lee, D.J.3    Yoon, Y.J.4    Kim, M.J.5    Shon, J.H.6    Choi, C.S.7    Choi, Y.K.8    Desta, Z.9    Shin, J.G.10
  • 64
    • 21344472349 scopus 로고    scopus 로고
    • Hydroxylation activity of P450 BM-3 mutant F87V towards aromatic compounds and its application to the synthesis of hydroquinone derivatives from phenolic compounds
    • Sulistyaningdyah WT, Ogawa J, Li QS, Maeda C, Yano Y, Schmid RD, Shimizu S (2005) Hydroxylation activity of P450 BM-3 mutant F87V towards aromatic compounds and its application to the synthesis of hydroquinone derivatives from phenolic compounds. Appl Microbiol Biotechnol 67:556-562.
    • (2005) Appl Microbiol Biotechnol , vol.67 , pp. 556-562
    • Sulistyaningdyah, W.T.1    Ogawa, J.2    Li, Q.S.3    Maeda, C.4    Yano, Y.5    Schmid, R.D.6    Shimizu, S.7
  • 65
    • 54949132112 scopus 로고    scopus 로고
    • Substrate binding to cytochromes P450
    • Isin EM, Guengerich FP (2008) Substrate binding to cytochromes P450. Anal Bioanal Chem 392:1019-1030.
    • (2008) Anal Bioanal Chem , vol.392 , pp. 1019-1030
    • Isin, E.M.1    Guengerich, F.P.2
  • 66
    • 33845379583 scopus 로고
    • Control of heme protein redox potential and reduction rate-linear free-energy relation between potential and ferric spin state equilibrium
    • Fisher MT, Sligar SG (1985) Control of heme protein redox potential and reduction rate-linear free-energy relation between potential and ferric spin state equilibrium. J Am Chem Soc 107:5018-5019.
    • (1985) J Am Chem Soc , vol.107 , pp. 5018-5019
    • Fisher, M.T.1    Sligar, S.G.2
  • 67
    • 0032479307 scopus 로고    scopus 로고
    • Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase
    • Bridges A, Gruenke L, Chang YT, Vakser IA, Loew G, Waskell L (1998) Identification of the binding site on cytochrome P450 2B4 for cytochrome b5 and cytochrome P450 reductase. J Biol Chem 273:17036-17049.
    • (1998) J Biol Chem , vol.273 , pp. 17036-17049
    • Bridges, A.1    Gruenke, L.2    Chang, Y.T.3    Vakser, I.A.4    Loew, G.5    Waskell, L.6
  • 68
    • 0027216444 scopus 로고
    • Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase
    • Shen S, Strobel HW (1993) Role of lysine and arginine residues of cytochrome P450 in the interaction between cytochrome P4502B1 and NADPH-cytochrome P450 reductase. Arch Biochem Biophys 304:257-265.
    • (1993) Arch Biochem Biophys , vol.304 , pp. 257-265
    • Shen, S.1    Strobel, H.W.2
  • 70
    • 0029763064 scopus 로고    scopus 로고
    • Approaches to crystallizing P450s
    • Poulos TL (1996) Approaches to crystallizing P450s. Methods Enzymol 272:358-368.
    • (1996) Methods Enzymol , vol.272 , pp. 358-368
    • Poulos, T.L.1
  • 73
    • 0035883794 scopus 로고    scopus 로고
    • Osmotic stress induced by carbohydrates enhances expression of foreign proteins in Escherichia coli
    • Kagawa N, Cao Q (2001) Osmotic stress induced by carbohydrates enhances expression of foreign proteins in Escherichia coli. Arch Biochem Biophys 393:290-296.
    • (2001) Arch Biochem Biophys , vol.393 , pp. 290-296
    • Kagawa, N.1    Cao, Q.2
  • 74
    • 45449113739 scopus 로고    scopus 로고
    • Bacterial expression and purification of interleukin-2 tyrosine kinase: Single step separation of the chaperonin impurity
    • Joseph RE, Andreotti AH (2008) Bacterial expression and purification of interleukin-2 tyrosine kinase: single step separation of the chaperonin impurity. Protein Expr Purif 60:194-197.
    • (2008) Protein Expr Purif , vol.60 , pp. 194-197
    • Joseph, R.E.1    Andreotti, A.H.2
  • 75
    • 0025302128 scopus 로고
    • Dual role of phospholipid in the reconstitution of cytochrome P-450 LM2-dependent activities
    • Causey KM, Eyer CS, Backes WL (1990) Dual role of phospholipid in the reconstitution of cytochrome P-450 LM2-dependent activities. Mol Pharmacol 38:134-142.
    • (1990) Mol Pharmacol , vol.38 , pp. 134-142
    • Causey, K.M.1    Eyer, C.S.2    Backes, W.L.3
  • 76
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • Kapust RB, Tozser J, Fox JD, Anderson DE, Cherry S, Copeland TD, Waugh D (2001) Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency. Protein Eng 14:993-1000.
    • (2001) Protein Eng , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tozser, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copeland, T.D.6    Waugh, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.