메뉴 건너뛰기




Volumn 3, Issue 2, 2013, Pages 395-402

Influence of foreign DNA introduction and periplasmic expression of recombinant human interleukin-2 on hydrogen peroxide quantity and catalase activity in Escherichia coli

Author keywords

Catalase activity; Escherichia coli; Hydrogen peroxide; Periplasmic expression; Recombinant protein

Indexed keywords

CATALASE; DNA; HYDROGEN PEROXIDE; RECOMBINANT INTERLEUKIN 2;

EID: 84885784009     PISSN: 22285881     EISSN: 22517308     Source Type: Journal    
DOI: 10.5681/apb.2013.063     Document Type: Article
Times cited : (2)

References (55)
  • 1
    • 0025405549 scopus 로고
    • Plasmid-encoded protein: the principal factor in the "metabolic burden" associated with recombinant bacteria
    • Bentley WE, Mirjalili N, Andersen DC, Davis RH, Kompala DS. Plasmid-encoded protein: the principal factor in the "metabolic burden" associated with recombinant bacteria. Biotechnol Bioeng 1990;35(7):668-81.
    • (1990) Biotechnol Bioeng , vol.35 , Issue.7 , pp. 668-681
    • Bentley, W.E.1    Mirjalili, N.2    Andersen, D.C.3    Davis, R.H.4    Kompala, D.S.5
  • 2
    • 0028801765 scopus 로고
    • Metabolic load and heterologous gene expression
    • Glick BR. Metabolic load and heterologous gene expression. Biotechnol Adv 1995;13(2):247-61.
    • (1995) Biotechnol Adv , vol.13 , Issue.2 , pp. 247-261
    • Glick, B.R.1
  • 3
    • 2942755215 scopus 로고    scopus 로고
    • Stress induced by recombinant protein production in Escherichia coli
    • Hoffmann F, Rinas U. Stress induced by recombinant protein production in Escherichia coli. Adv Biochem Eng Biotechnol 2004;89:73-92.
    • (2004) Adv Biochem Eng Biotechnol , vol.89 , pp. 73-92
    • Hoffmann, F.1    Rinas, U.2
  • 4
    • 84906264700 scopus 로고    scopus 로고
    • Bacterial stress response
    • In: Rosenberg E, DeLong E, Lory S, Stackebrandt E, Thompson F, editors. The prokaryotes. 4th ed. Berlin: Springer;
    • Ron EZ. Bacterial stress response. In: Rosenberg E, DeLong E, Lory S, Stackebrandt E, Thompson F, editors. The prokaryotes. 4th ed. Berlin: Springer; 2013. P. 589-603.
    • (2013) , pp. 589-603
    • Ron, E.Z.1
  • 5
    • 34548012600 scopus 로고    scopus 로고
    • Engineering cell physiology to enhance recombinant protein production in Escherichia coli
    • Chou CP. Engineering cell physiology to enhance recombinant protein production in Escherichia coli. Appl Microbiol Biotechnol 2007;76(3):521-32.
    • (2007) Appl Microbiol Biotechnol , vol.76 , Issue.3 , pp. 521-532
    • Chou, C.P.1
  • 6
    • 33845315054 scopus 로고    scopus 로고
    • Effects of the presence of ColE1 plasmid DNA in Escherichia coli on the host cell metabolism
    • Wang Z, Xiang L, Shao J, Wegrzyn A, Wegrzyn G. Effects of the presence of ColE1 plasmid DNA in Escherichia coli on the host cell metabolism. Microb Cell Fact 2006;5:34.
    • (2006) Microb Cell Fact , vol.5 , pp. 34
    • Wang, Z.1    Xiang, L.2    Shao, J.3    Wegrzyn, A.4    Wegrzyn, G.5
  • 7
    • 0037137907 scopus 로고    scopus 로고
    • Stabilizing plasmid copy number to improve recombinant protein production
    • Grabherr R, Nilsson E, Striedner G, Bayer K. Stabilizing plasmid copy number to improve recombinant protein production. Biotechnol Bioeng 2002;77(2):142-7.
    • (2002) Biotechnol Bioeng , vol.77 , Issue.2 , pp. 142-147
    • Grabherr, R.1    Nilsson, E.2    Striedner, G.3    Bayer, K.4
  • 8
    • 0037473189 scopus 로고    scopus 로고
    • Combined transcriptome and proteome analysis of Escherichia coli during high cell density culture
    • Yoon SH, Han MJ, Lee SY, Jeong KJ, Yoo JS. Combined transcriptome and proteome analysis of Escherichia coli during high cell density culture. Biotechnol Bioeng 2003;81(7):753-67.
    • (2003) Biotechnol Bioeng , vol.81 , Issue.7 , pp. 753-767
    • Yoon, S.H.1    Han, M.J.2    Lee, S.Y.3    Jeong, K.J.4    Yoo, J.S.5
  • 9
    • 0344521722 scopus 로고    scopus 로고
    • Protein Purification Protocols
    • Yip TT, Hutchens TW, editors, Totowa, NJ: Humana Press Inc
    • Doonan S. Protein Purification Protocols. In: Yip TT, Hutchens TW, editors. Methods in Molecular Biology. Totowa, NJ: Humana Press Inc;1996. P. 57-75.
    • (1996) Methods in Molecular Biology , pp. 57-75
    • Doonan, S.1
  • 10
    • 0141908145 scopus 로고    scopus 로고
    • Optimization of an osmotic shock procedure for isolation of a protein product expressed in E
    • Rathore AS, Bilbrey RE, Steinmeyer DE. Optimization of an osmotic shock procedure for isolation of a protein product expressed in E. coli. Biotechnol Prog 2003;19(5):1541-6.
    • (2003) coli. Biotechnol Prog , vol.19 , Issue.5 , pp. 1541-1546
    • Rathore, A.S.1    Bilbrey, R.E.2    Steinmeyer, D.E.3
  • 11
    • 27844561706 scopus 로고    scopus 로고
    • The selection of optimum media formulations for improved expression of recombinant proteins in E
    • Broedel SE, Papciak, SM, Jones WR. The selection of optimum media formulations for improved expression of recombinant proteins in E. coli. Tech Bull 2001;2:1-7.
    • (2001) coli. Tech Bull , vol.2 , pp. 1-7
    • Broedel, S.E.1    Papciak, S.M.2    Jones, W.R.3
  • 12
    • 33646082049 scopus 로고    scopus 로고
    • Replacement of the glucose phosphotransferase transport system by galactose permease reduces acetate accumulation and improves process performance of Escherichia coli for recombinant protein production without impairment of growth rate
    • De Anda R, Lara AR, Hernandez V, Hernandez-Montalvo V, Gosset G, Bolivar F, et al. Replacement of the glucose phosphotransferase transport system by galactose permease reduces acetate accumulation and improves process performance of Escherichia coli for recombinant protein production without impairment of growth rate. Metab Eng 2006;8(3):281-90.
    • (2006) Metab Eng , vol.8 , Issue.3 , pp. 281-290
    • De Anda, R.1    Lara, A.R.2    Hernandez, V.3    Hernandez-Montalvo, V.4    Gosset, G.5    Bolivar, F.6
  • 13
    • 33745186217 scopus 로고    scopus 로고
    • Increased recombinant protein production in Escherichia coli strains with overexpressed water-forming NADH oxidase and a deleted ArcA regulatory protein
    • Vemuri GN, Eiteman MA, Altman E. Increased recombinant protein production in Escherichia coli strains with overexpressed water-forming NADH oxidase and a deleted ArcA regulatory protein. Biotechnol Bioeng 2006;94(3):538-42.
    • (2006) Biotechnol Bioeng , vol.94 , Issue.3 , pp. 538-542
    • Vemuri, G.N.1    Eiteman, M.A.2    Altman, E.3
  • 14
    • 17644394580 scopus 로고    scopus 로고
    • Reducing the glucose uptake rate in Escherichia coli affects growth rate but not protein production
    • Picon A, Teixeira De Mattos MJ, Postma PW. Reducing the glucose uptake rate in Escherichia coli affects growth rate but not protein production. Biotechnol Bioeng 2005;90(2):191-200.
    • (2005) Biotechnol Bioeng , vol.90 , Issue.2 , pp. 191-200
    • Picon, A.1    Teixeira De Mattos, M.J.2    Postma, P.W.3
  • 15
    • 26844512919 scopus 로고    scopus 로고
    • Improvement of Escherichia coli production strains by modification of the phosphoenolpyruvate:sugar phosphotransferase system
    • Gosset G. Improvement of Escherichia coli production strains by modification of the phosphoenolpyruvate:sugar phosphotransferase system. Microb Cell Fact 2005;4(1):14.
    • (2005) Microb Cell Fact , vol.4 , Issue.1 , pp. 14
    • Gosset, G.1
  • 16
    • 3042553661 scopus 로고    scopus 로고
    • Constitutive production of human leptin by fed-batch culture of recombinant rpoS-Escherichia coli
    • Jeong KJ, Choi JH, Yoo WM, Keum KC, Yoo NC, Lee SY, et al. Constitutive production of human leptin by fed-batch culture of recombinant rpoS-Escherichia coli. Protein Expr Purif 2004;36(1):150-6.
    • (2004) Protein Expr Purif , vol.36 , Issue.1 , pp. 150-156
    • Jeong, K.J.1    Choi, J.H.2    Yoo, W.M.3    Keum, K.C.4    Yoo, N.C.5    Lee, S.Y.6
  • 17
    • 29144469368 scopus 로고    scopus 로고
    • Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones
    • De Marco A, Vigh L, Diamant S, Goloubinoff P. Native folding of aggregation-prone recombinant proteins in Escherichia coli by osmolytes, plasmid- or benzyl alcohol-overexpressed molecular chaperones. Cell Stress Chaperones 2005;10(4):329-39.
    • (2005) Cell Stress Chaperones , vol.10 , Issue.4 , pp. 329-339
    • De Marco, A.1    Vigh, L.2    Diamant, S.3    Goloubinoff, P.4
  • 18
    • 23244464653 scopus 로고    scopus 로고
    • The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies
    • Lethanh H, Neubauer P, Hoffmann F. The small heat-shock proteins IbpA and IbpB reduce the stress load of recombinant Escherichia coli and delay degradation of inclusion bodies. Microb Cell Fact 2005;4(1):6.
    • (2005) Microb Cell Fact , vol.4 , Issue.1 , pp. 6
    • Lethanh, H.1    Neubauer, P.2    Hoffmann, F.3
  • 19
    • 0034152767 scopus 로고    scopus 로고
    • Oxidative stress in bacteria and protein damage by reactive oxygen species
    • Cabiscol E, Tamarit J, Ros J. Oxidative stress in bacteria and protein damage by reactive oxygen species. Int Microbiol 2000;3(1):3-8.
    • (2000) Int Microbiol , vol.3 , Issue.1 , pp. 3-8
    • Cabiscol, E.1    Tamarit, J.2    Ros, J.3
  • 20
    • 78650598564 scopus 로고    scopus 로고
    • Adaptive response to oxidative stress: Bacteria, fungi, plants and animals
    • Lushchak VI. Adaptive response to oxidative stress: Bacteria, fungi, plants and animals. Comp Biochem Physiol C Toxicol Pharmacol 2011;153(2):175-90.
    • (2011) Comp Biochem Physiol C Toxicol Pharmacol , vol.153 , Issue.2 , pp. 175-190
    • Lushchak, V.I.1
  • 21
    • 77954040167 scopus 로고    scopus 로고
    • Molecular cloning and expression analysis of an Mn-SOD gene from Nelumbo nucifera
    • Dong C, Li G, Li Z, Zhu H, Zhou M, Hu Z. Molecular cloning and expression analysis of an Mn-SOD gene from Nelumbo nucifera. Appl Biochem Biotechnol 2009;158(3):605-14.
    • (2009) Appl Biochem Biotechnol , vol.158 , Issue.3 , pp. 605-614
    • Dong, C.1    Li, G.2    Li, Z.3    Zhu, H.4    Zhou, M.5    Hu, Z.6
  • 22
    • 79952705700 scopus 로고    scopus 로고
    • Molecular cloning and expression of two cytosolic copper-zinc superoxide dismutases genes from Nelumbo nucifera
    • Dong C, Zheng X, Li G, Zhu H, Zhou M, Hu Z. Molecular cloning and expression of two cytosolic copper-zinc superoxide dismutases genes from Nelumbo nucifera. Appl Biochem Biotechnol 2011;163(5):679-91.
    • (2011) Appl Biochem Biotechnol , vol.163 , Issue.5 , pp. 679-691
    • Dong, C.1    Zheng, X.2    Li, G.3    Zhu, H.4    Zhou, M.5    Hu, Z.6
  • 23
    • 80052434027 scopus 로고    scopus 로고
    • Biochemical studies on hemoglobin modified with reactive oxygen species (ROS)
    • Khaket TP, Ahmad R. Biochemical studies on hemoglobin modified with reactive oxygen species (ROS). Appl Biochem Biotechnol 2011;164(8):1422-30.
    • (2011) Appl Biochem Biotechnol , vol.164 , Issue.8 , pp. 1422-1430
    • Khaket, T.P.1    Ahmad, R.2
  • 24
    • 0030049032 scopus 로고    scopus 로고
    • Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer
    • Wiseman H, Halliwell B. Damage to DNA by reactive oxygen and nitrogen species: role in inflammatory disease and progression to cancer. Biochem J 1996;313 ( Pt 1):17-29.
    • (1996) Biochem J , vol.313 , Issue.PART 1 , pp. 17-29
    • Wiseman, H.1    Halliwell, B.2
  • 25
    • 0025674536 scopus 로고
    • Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences
    • Stadtman ER. Metal ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Radic Biol Med 1990;9(4):315-25.
    • (1990) Free Radic Biol Med , vol.9 , Issue.4 , pp. 315-325
    • Stadtman, E.R.1
  • 26
    • 3242752786 scopus 로고    scopus 로고
    • Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells
    • Boonstra J, Post JA. Molecular events associated with reactive oxygen species and cell cycle progression in mammalian cells. Gene 2004;337:1-13.
    • (2004) Gene , vol.337 , pp. 1-13
    • Boonstra, J.1    Post, J.A.2
  • 27
    • 23644459809 scopus 로고    scopus 로고
    • Acid stress adaptation protects Saccharomyces cerevisiae from acetic acid-induced programmed cell death
    • Giannattasio S, Guaragnella N, Corte-Real M, Passarella S, Marra E. Acid stress adaptation protects Saccharomyces cerevisiae from acetic acid-induced programmed cell death. Gene 2005;354:93-8.
    • (2005) Gene , vol.354 , pp. 93-98
    • Giannattasio, S.1    Guaragnella, N.2    Corte-Real, M.3    Passarella, S.4    Marra, E.5
  • 28
    • 14044271464 scopus 로고    scopus 로고
    • Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli
    • Hondorp ER, Matthews RG. Oxidative stress inactivates cobalamin-independent methionine synthase (MetE) in Escherichia coli. PLoS Biol 2004;2(11):e336.
    • (2004) PLoS Biol , vol.2 , Issue.11
    • Hondorp, E.R.1    Matthews, R.G.2
  • 29
    • 14044257165 scopus 로고    scopus 로고
    • Protein thiol modifications visualized in vivo
    • Leichert LI, Jakob U. Protein thiol modifications visualized in vivo. PLoS Biol 2004;2(11):e333.
    • (2004) PLoS Biol , vol.2 , Issue.11
    • Leichert, L.I.1    Jakob, U.2
  • 30
    • 0029018721 scopus 로고
    • Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli
    • Gonzalez-Flecha B, Demple B. Metabolic sources of hydrogen peroxide in aerobically growing Escherichia coli. J Biol Chem 1995;270(23):13681-7.
    • (1995) J Biol Chem , vol.270 , Issue.23 , pp. 13681-13687
    • Gonzalez-Flecha, B.1    Demple, B.2
  • 31
    • 0031025115 scopus 로고    scopus 로고
    • Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli
    • Gonzalez-Flecha B, Demple B. Homeostatic regulation of intracellular hydrogen peroxide concentration in aerobically growing Escherichia coli. J Bacteriol 1997;179(2):382-8.
    • (1997) J Bacteriol , vol.179 , Issue.2 , pp. 382-388
    • Gonzalez-Flecha, B.1    Demple, B.2
  • 32
    • 0026074553 scopus 로고
    • Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII
    • Von Ossowski I, Mulvey MR, Leco PA, Borys A, Loewen PC. Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII. J Bacteriol 1991;173(2):514-20.
    • (1991) J Bacteriol , vol.173 , Issue.2 , pp. 514-520
    • Von Ossowski, I.1    Mulvey, M.R.2    Leco, P.A.3    Borys, A.4    Loewen, P.C.5
  • 33
    • 0022366614 scopus 로고
    • Catalases HPI and HPII in Escherichia coli are induced independently
    • Loewen PC, Switala J, Triggs-Raine BL. Catalases HPI and HPII in Escherichia coli are induced independently. Arch Biochem Biophys 1985;243(1):144-9.
    • (1985) Arch Biochem Biophys , vol.243 , Issue.1 , pp. 144-149
    • Loewen, P.C.1    Switala, J.2    Triggs-Raine, B.L.3
  • 34
    • 0033772459 scopus 로고    scopus 로고
    • Expressing genes in different Escherichia coli compartments
    • Cornelis P. Expressing genes in different Escherichia coli compartments. Curr Opin Biotechnol 2000;11(5):450-4.
    • (2000) Curr Opin Biotechnol , vol.11 , Issue.5 , pp. 450-454
    • Cornelis, P.1
  • 35
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol 1999;10(5):411-21.
    • (1999) Curr Opin Biotechnol , vol.10 , Issue.5 , pp. 411-421
    • Baneyx, F.1
  • 36
    • 33645881071 scopus 로고    scopus 로고
    • Pathways of disulfide bond formation in Escherichia coli
    • Messens J, Collet JF. Pathways of disulfide bond formation in Escherichia coli. Int J Biochem Cell Biol 2006;38(7):1050-62.
    • (2006) Int J Biochem Cell Biol , vol.38 , Issue.7 , pp. 1050-1062
    • Messens, J.1    Collet, J.F.2
  • 37
    • 0030444320 scopus 로고    scopus 로고
    • Proteases and their targets in Escherichia coli
    • Gottesman S. Proteases and their targets in Escherichia coli. Annu Rev Genet 1996;30:465-506.
    • (1996) Annu Rev Genet , vol.30 , pp. 465-506
    • Gottesman, S.1
  • 38
    • 0037360296 scopus 로고    scopus 로고
    • Expression of proteins using the third domain of the Escherichia coli periplasmic-protein TolA as a fusion partner
    • Anderluh G, Gokce I, Lakey JH. Expression of proteins using the third domain of the Escherichia coli periplasmic-protein TolA as a fusion partner. Protein Expres Purif 2003;28(1):173-81.
    • (2003) Protein Expres Purif , vol.28 , Issue.1 , pp. 173-181
    • Anderluh, G.1    Gokce, I.2    Lakey, J.H.3
  • 39
    • 0028032403 scopus 로고
    • Escherichia coli expresses a copper- and zinc-containing superoxide dismutase
    • Benov LT, Fridovich I. Escherichia coli expresses a copper- and zinc-containing superoxide dismutase. J Biol Chem 1994;269(41):25310-4.
    • (1994) J Biol Chem , vol.269 , Issue.41 , pp. 25310-25314
    • Benov, L.T.1    Fridovich, I.2
  • 41
    • 0033118280 scopus 로고    scopus 로고
    • Starvation, cessation of growth and bacterial aging
    • Nystrom T. Starvation, cessation of growth and bacterial aging. Curr Opin Microbiol 1999;2(2):214-9.
    • (1999) Curr Opin Microbiol , vol.2 , Issue.2 , pp. 214-219
    • Nystrom, T.1
  • 44
    • 68949136469 scopus 로고    scopus 로고
    • Cytoplasmic expression of recombinant interleukin-2 and interleukin-4 proteins results in hydrogen peroxide accumulation and reduction in catalase activity in Escherichia coli
    • Hejazi MS, Karimi F, Mehdizadeh Aghdam E, Barzegari A, Farshdosti Hagh M, Parvizi M, et al. Cytoplasmic expression of recombinant interleukin-2 and interleukin-4 proteins results in hydrogen peroxide accumulation and reduction in catalase activity in Escherichia coli. DARU 2009;17(2):64-71.
    • (2009) DARU , vol.17 , Issue.2 , pp. 64-71
    • Hejazi, M.S.1    Karimi, F.2    Mehdizadeh Aghdam, E.3    Barzegari, A.4    Farshdosti Hagh, M.5    Parvizi, M.6
  • 45
    • 84868215173 scopus 로고    scopus 로고
    • Effect of periplasmic expression of recombinant mouse interleukin-4 on hydrogen peroxide concentration and catalase activity in Escherichia coli
    • Mehdizadeh Aghdam E, Mahmoudi Azar L, Barzegari A, Karimi F, Mesbahfar M, Samadi N, et al. Effect of periplasmic expression of recombinant mouse interleukin-4 on hydrogen peroxide concentration and catalase activity in Escherichia coli. Gene 2012;511(2):455-60.
    • (2012) Gene , vol.511 , Issue.2 , pp. 455-460
    • Mehdizadeh Aghdam, E.1    Mahmoudi Azar, L.2    Barzegari, A.3    Karimi, F.4    Mesbahfar, M.5    Samadi, N.6
  • 46
    • 0034615020 scopus 로고    scopus 로고
    • Oxidative stress and some antioxidant systems in acid raintreated bean plants- Protective role of exogenous polyamines
    • Velikova V, Yordanov I, Edreva A. Oxidative stress and some antioxidant systems in acid raintreated bean plants- Protective role of exogenous polyamines. Plant Sci 2000;151(1):59-66.
    • (2000) Plant Sci , vol.151 , Issue.1 , pp. 59-66
    • Velikova, V.1    Yordanov, I.2    Edreva, A.3
  • 47
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 48
    • 31144471322 scopus 로고    scopus 로고
    • Bacterial stress responses: what doesn't kill them can make then stronger
    • Boor KJ. Bacterial stress responses: what doesn't kill them can make then stronger. PLoS Biol 2006;4(1):e23.
    • (2006) PLoS Biol , vol.4 , Issue.1
    • Boor, K.J.1
  • 49
    • 0037255508 scopus 로고    scopus 로고
    • Construction of a sodA::luxCDABE fusion Escherichia coli: comparison with a katG fusion strain through their responses to oxidative stresses
    • Lee HJ, Gu MB. Construction of a sodA::luxCDABE fusion Escherichia coli: comparison with a katG fusion strain through their responses to oxidative stresses. Appl Microbiol Biotechnol 2003;60(5):577-80.
    • (2003) Appl Microbiol Biotechnol , vol.60 , Issue.5 , pp. 577-580
    • Lee, H.J.1    Gu, M.B.2
  • 50
    • 25844514728 scopus 로고    scopus 로고
    • Preparative expression of secreted proteins in bacteria: status report and future prospects
    • Georgiou G, Segatori L. Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr Opin Biotechnol 2005;16(5):538-45.
    • (2005) Curr Opin Biotechnol , vol.16 , Issue.5 , pp. 538-545
    • Georgiou, G.1    Segatori, L.2
  • 51
    • 0037029129 scopus 로고    scopus 로고
    • Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage
    • Paradies G, Petrosillo G, Pistolese M, Ruggiero FM. Reactive oxygen species affect mitochondrial electron transport complex I activity through oxidative cardiolipin damage. Gene 2002;286(1):135-41.
    • (2002) Gene , vol.286 , Issue.1 , pp. 135-141
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Ruggiero, F.M.4
  • 52
    • 0035773684 scopus 로고    scopus 로고
    • Oxidative stress and mechanisms of protection against it in bacteria
    • Lushchak VI. Oxidative stress and mechanisms of protection against it in bacteria. Biochemistry (Mosc) 2001;66(5):476-89.
    • (2001) Biochemistry (Mosc) , vol.66 , Issue.5 , pp. 476-489
    • Lushchak, V.I.1
  • 53
    • 84885828848 scopus 로고    scopus 로고
    • Advanced genetic strategies for expression recombinant potein in Escherichia coli
    • Hans PS, Kim Kusk M. Advanced genetic strategies for expression recombinant potein in Escherichia coli. J Biotechnol 2004;14:113-28
    • (2004) J Biotechnol , vol.14 , pp. 113-128
    • Hans, P.S.1    Kim Kusk, M.2
  • 54
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides SC. Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev 1996;60(3):512-38.
    • (1996) Microbiol Rev , vol.60 , Issue.3 , pp. 512-538
    • Makrides, S.C.1
  • 55
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier FW, Moffatt BA. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 1986;189(1):113-30.
    • (1986) J Mol Biol , vol.189 , Issue.1 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.