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Volumn 47, Issue 2, 2011, Pages 111-119

Production of hepatopoietin Cn in high-cell-density cultures of recombinant Escherichia coli and detection of its antioxygen activity

Author keywords

Antioxygen; Hepatopoietin Cn; High cell density fermentation; Recombinant protein; Renaturation

Indexed keywords

ANTIOXYGEN; HEPATOPOIETIN CN; HIGH-CELL-DENSITY FERMENTATION; RECOMBINANT PROTEIN; RENATURATION;

EID: 79551535519     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12033-010-9318-x     Document Type: Article
Times cited : (3)

References (24)
  • 2
    • 59149102122 scopus 로고    scopus 로고
    • The protective role of Hepatopoietin Cn on liver injury induced by carbon tetrachloride in rats
    • 10.1111/j.1872-034X.2008.00447.x 1:CAS:528:DC%2BD1MXjvVygs78%3D 10.1111/j.1872-034X.2008.00447.x
    • CP Cui P Wei Y Liu DJ Zhang LS Wang CT Wu 2009 The protective role of Hepatopoietin Cn on liver injury induced by carbon tetrachloride in rats Hepatology Research 39 200 206 10.1111/j.1872-034X.2008.00447.x 1:CAS:528:DC%2BD1MXjvVygs78%3D 10.1111/j.1872-034X.2008.00447.x
    • (2009) Hepatology Research , vol.39 , pp. 200-206
    • Cui, C.P.1    Wei, P.2    Liu, Y.3    Zhang, D.J.4    Wang, L.S.5    Wu, C.T.6
  • 3
    • 0029874193 scopus 로고    scopus 로고
    • High cell-density culture of Escherichia coli
    • DOI 10.1016/0167-7799(96)80930-9
    • SY Lee 1996 High cell-density culture of Escherichia coli Trends in Biotechnology 14 98 105 10.1016/0167-7799(96)80930-9 1:CAS:528: DyaK28XhsleqtLs%3D 10.1016/0167-7799(96)80930-9 (Pubitemid 26079509)
    • (1996) Trends in Biotechnology , vol.14 , Issue.3 , pp. 98-105
    • Lee, S.Y.1
  • 4
    • 0027015640 scopus 로고
    • Recombinant protein expression in high cell density fed-batch cultures of Escherichia coli
    • 10.1038/nbt1292-1550 1:CAS:528:DyaK3sXhtVSns70%3D 10.1038/nbt1292-1550
    • L Yee HW Blanch 1992 Recombinant protein expression in high cell density fed-batch cultures of Escherichia coli Biotechnology (NY) 10 1550 1556 10.1038/nbt1292-1550 1:CAS:528:DyaK3sXhtVSns70%3D 10.1038/nbt1292-1550
    • (1992) Biotechnology (NY) , vol.10 , pp. 1550-1556
    • Yee, L.1    Blanch, H.W.2
  • 5
    • 3042591780 scopus 로고    scopus 로고
    • High-level expression of a fungal pyranose oxidase in high cell-density fed-batch cultivations of Escherichia coli using lactose as inducer
    • DOI 10.1016/j.pep.2004.02.011, PII S1046592804000877
    • M Kotik M Kocanova H Maresova P Kyslik 2004 High-level expression of a fungal pyranose oxidase in high cell-density fed-batch cultivations of Escherichia coli using lactose as inducer Protein Expression and Purification 36 61 69 10.1016/j.pep.2004.02.011 1:CAS:528:DC%2BD2cXks1ersrk%3D 10.1016/j.pep.2004.02.011 (Pubitemid 38836765)
    • (2004) Protein Expression and Purification , vol.36 , Issue.1 , pp. 61-69
    • Kotik, M.1    Kocanova, M.2    Maresova, H.3    Kyslik, P.4
  • 6
    • 70849085440 scopus 로고    scopus 로고
    • Application of a fed-batch bioprocess for the heterologous production of hSCOMT in Escherichia coli
    • 1:CAS:528:DC%2BD1MXhtlansrjP 10.4014/jmb.0812.658 PMid: 19809255
    • LA Passarinha MJ Bonifacio JA Queiroz 2009 Application of a fed-batch bioprocess for the heterologous production of hSCOMT in Escherichia coli Journal of Microbiology and Biotechnology 19 972 981 1:CAS:528:DC%2BD1MXhtlansrjP 10.4014/jmb.0812.658 PMid: 19809255
    • (2009) Journal of Microbiology and Biotechnology , vol.19 , pp. 972-981
    • Passarinha, L.A.1    Bonifacio, M.J.2    Queiroz, J.A.3
  • 7
    • 0036271397 scopus 로고    scopus 로고
    • Industrial control of recombinant E. coli fed-batch culture: New perspectives on traditional controlled variables
    • DOI 10.1007/s00449-002-0287-8
    • W Johnston R Cord-Ruwisch MJ Cooney 2002 Industrial control of recombinant E. coli fed-batch culture: New perspectives on traditional controlled variables Bioprocess and Biosystems Engineering 25 111 120 10.1007/s00449-002-0287-8 1:CAS:528:DC%2BD38XktFarsbw%3D 10.1007/s00449-002- 0287-8 (Pubitemid 34595831)
    • (2002) Bioprocess and Biosystems Engineering , vol.25 , Issue.2 , pp. 111-120
    • Johnston, W.1    Cord-Ruwisch, R.2    Cooney, M.J.3
  • 8
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • 10.1263/jbb.99.303 1:CAS:528:DC%2BD2MXlsFCnsrc%3D 10.1263/jbb.99.303
    • SM Singh AK Panda 2005 Solubilization and refolding of bacterial inclusion body proteins Journal of Bioscience and Bioengineering 99 303 310 10.1263/jbb.99.303 1:CAS:528:DC%2BD2MXlsFCnsrc%3D 10.1263/jbb.99.303
    • (2005) Journal of Bioscience and Bioengineering , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 9
    • 0025826932 scopus 로고
    • High cell density cultivation of Escherichia coli at controlled specific growth rate
    • 10.1016/0168-1656(91)90032-Q 1:CAS:528:DyaK3MXltFakurs%3D 10.1016/0168-1656(91)90032-Q
    • D Riesenberg V Schulz WA Knorre HD Pohl D Korz EA Sanders A Ross WD Deckwer 1991 High cell density cultivation of Escherichia coli at controlled specific growth rate Journal of Biotechnology 20 17 27 10.1016/0168-1656(91) 90032-Q 1:CAS:528:DyaK3MXltFakurs%3D 10.1016/0168-1656(91)90032-Q
    • (1991) Journal of Biotechnology , vol.20 , pp. 17-27
    • Riesenberg, D.1    Schulz, V.2    Knorre, W.A.3    Pohl, H.D.4    Korz, D.5    Sanders, E.A.6    Ross, A.7    Deckwer, W.D.8
  • 10
    • 0038227075 scopus 로고    scopus 로고
    • Renaturation of heterodimeric platelet-derived growth factor from inclusion bodies of recombinant Escherichia coli using size-exclusion chromatography
    • DOI 10.1016/S0021-9673(99)00660-3, PII S0021967399006603
    • C Muller U Rinas 1999 Renaturation of heterodimeric platelet-derived growth factor from inclusion bodies of recombinant Escherichia coli using size-exclusion chromatography Journal of Chromatography A 855 203 213 10.1016/S0021-9673(99)00660-3 1:CAS:528:DyaK1MXmsFWrsL4%3D 10.1016/S0021- 9673(99)00660-3 (Pubitemid 29413099)
    • (1999) Journal of Chromatography A , vol.855 , Issue.1 , pp. 203-213
    • Muller, C.1    Rinas, U.2
  • 11
    • 0037187447 scopus 로고    scopus 로고
    • Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli
    • DOI 10.1016/S0168-1656(01)00425-4, PII S0168165601004254
    • LF Vallejo M Brokelmann S Marten S Trappe J Cabrera-Crespo A Hoffmann G Gross HA Weich U Rinas 2002 Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli Journal of Biotechnology 94 185 194 10.1016/S0168-1656(01)00425-4 1:CAS:528:DC%2BD38XktFSqsA%3D%3D 10.1016/S0168-1656(01)00425-4 (Pubitemid 34127660)
    • (2002) Journal of Biotechnology , vol.94 , Issue.2 , pp. 185-194
    • Vallejo, L.F.1    Brokelmann, M.2    Marten, S.3    Trappe, S.4    Cabrera-Crespo, J.5    Hoffmann, A.6    Gross, G.7    Weich, H.A.8    Rinas, U.9
  • 12
    • 13844297856 scopus 로고    scopus 로고
    • Purification and on-column refolding of EGFP overexpressed as inclusion bodies in Escherichia coli with expanded bed anion exchange chromatography
    • DOI 10.1016/j.jchromb.2004.10.023, PII S1570023204008165
    • C Cabanne AM Noubhani A Hocquellet F Dole W Dieryck X Santarelli 2005 Purification and on-column refolding of EGFP overexpressed as inclusion bodies in Escherichia coli with expanded bed anion exchange chromatography Journal of Chromatography B (Analytical Technologies in the Biomedical and Life Sciences) 818 23 27 10.1016/j.jchromb.2004.10.023 1:CAS:528:DC%2BD2MXhsVKqurY%3D 10.1016/j.jchromb.2004.10.023 (Pubitemid 40249622)
    • (2005) Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences , vol.818 , Issue.1 SPEC. ISSUE , pp. 23-27
    • Cabanne, C.1    Noubhani, A.M.2    Hocquellet, A.3    Dole, F.4    Dieryck, W.5    Santarelli, X.6
  • 13
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies
    • DOI 10.1016/S0168-1656(96)01636-7, PII S0168165696016367
    • D Arora N Khanna 1996 Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies Journal of Biotechnology 52 127 133 10.1016/S0168-1656(96)01636-7 1:CAS:528: DyaK2sXptlWisg%3D%3D 10.1016/S0168-1656(96)01636-7 (Pubitemid 27141634)
    • (1996) Journal of Biotechnology , vol.52 , Issue.2 , pp. 127-133
    • Arora, D.1    Khanna, N.2
  • 14
    • 0037428060 scopus 로고    scopus 로고
    • Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells role of transferrin receptor-dependent iron uptake in apoptosis
    • DOI 10.1161/01.RES.0000048195.15637.AC
    • Y Tampo S Kotamraju CR Chitambar SV Kalivendi A Keszler J Joseph B Kalyanaraman 2003 Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: Role of transferrin receptor-dependent iron uptake in apoptosis Circulation Research 92 56 63 10.1161/01.RES.0000048195.15637.AC 1:CAS:528:DC%2BD3sXmvFE%3D 10.1161/01.RES.0000048195.15637.AC (Pubitemid 36105607)
    • (2003) Circulation Research , vol.92 , Issue.1 , pp. 56-63
    • Tampo, Y.1    Kotamraju, S.2    Chitambar, C.R.3    Kalivendi, S.V.4    Keszler, A.5    Kalyanaraman, J.J.B.6
  • 15
    • 0029055426 scopus 로고
    • A novel activity of OmpT. Proteolysis under extreme denaturing conditions
    • 1:CAS:528:DyaK2MXmtV2it7w%3D 10.1074/jbc.270.22.12990 PMID: 7768890
    • CB White Q Chen GL Kenyon PC Babbitt 1995 A novel activity of OmpT. Proteolysis under extreme denaturing conditions The Journal of Biological Chemistry 270 12990 12994 1:CAS:528:DyaK2MXmtV2it7w%3D 10.1074/jbc.270.22.12990 PMID: 7768890
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 12990-12994
    • White, C.B.1    Chen, Q.2    Kenyon, G.L.3    Babbitt, P.C.4
  • 16
    • 0035313153 scopus 로고    scopus 로고
    • Advances in Escherichia coli production of therapeutic proteins
    • DOI 10.1016/S0958-1669(00)00199-3
    • JR Swartz 2001 Advances in Escherichia coli production of therapeutic proteins Current Opinion in Biotechnology 12 195 201 10.1016/S0958-1669(00) 00199-3 1:CAS:528:DC%2BD3MXjt1Oksr4%3D 10.1016/S0958-1669(00)00199-3 (Pubitemid 32247408)
    • (2001) Current Opinion in Biotechnology , vol.12 , Issue.2 , pp. 195-201
    • Swartz, J.R.1
  • 17
    • 0016769993 scopus 로고
    • Preparation and partial characterization of hepatic regenerative stimulator substance (SS) from rat liver
    • 1:CAS:528:DyaE2MXkt1ekur8%3D (PMid:1151784)
    • DR LaBrecque LA Pesch 1975 Preparation and partial characterization of hepatic regenerative stimulator substance (SS) from rat liver Journal of Physiology 248 273 284 1:CAS:528:DyaE2MXkt1ekur8%3D (PMid:1151784)
    • (1975) Journal of Physiology , vol.248 , pp. 273-284
    • Labrecque, D.R.1    Pesch, L.A.2
  • 18
    • 27744471883 scopus 로고    scopus 로고
    • Expression of the pyranose 2-oxidase from Trametes pubescens in Escherichia coli and characterization of the recombinant enzyme
    • DOI 10.1016/j.jbiotec.2005.06.021, PII S0168165605003354
    • H Maresová B Vecerek M Hradská N Libessart S Becka MH Saniez P Kyslík 2005 Expression of the pyranose 2-oxidase from Trametes pubescens in Escherichia coli and characterization of the recombinant enzyme Journal of Biotechnology 120 387 395 10.1016/j.jbiotec.2005.06.021 10.1016/j.jbiotec.2005.06.021 (Pubitemid 41627968)
    • (2005) Journal of Biotechnology , vol.120 , Issue.4 , pp. 387-395
    • Maresova, H.1    Vecerek, B.2    Hradska, M.3    Libessart, N.4    Becka, S.5    Saniez, M.-H.6    Kyslik, P.7
  • 19
    • 0025264582 scopus 로고
    • Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations
    • 1:CAS:528:DyaK3cXitleqtb8%3D (PMid:2187400)
    • GW Luli WR Strohl 1990 Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations Applied and Environmental Microbiology 56 1004 1011 1:CAS:528:DyaK3cXitleqtb8%3D (PMid:2187400)
    • (1990) Applied and Environmental Microbiology , vol.56 , pp. 1004-1011
    • Luli, G.W.1    Strohl, W.R.2
  • 20
    • 0029892121 scopus 로고    scopus 로고
    • Review: Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter
    • DOI 10.1007/BF01569997
    • RS Donovan CW Robinson BR Glick 1996 Review: optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter Journal of Industrial Microbiology 16 145 154 10.1007/BF01569997 1:CAS:528:DyaK28XisFSkt7s%3D 10.1007/BF01569997 (Pubitemid 26139630)
    • (1996) Journal of Industrial Microbiology , vol.16 , Issue.3 , pp. 145-154
    • Donovan, R.S.1    Robinson, C.W.2    Click, B.R.3
  • 21
    • 7044228084 scopus 로고    scopus 로고
    • Protein expression and refolding - A practical guide to getting the most out of inclusion bodies
    • DOI 10.1016/S1387-2656(04)10002-1, PII S1387265604100021
    • LD Cabrita SP Bottomley 2004 Protein expression and refolding-a practical guide to getting the most out of inclusion bodies Biotechnology Annual Review 10 31 50 10.1016/S1387-2656(04)10002-1 1:CAS:528:DC%2BD1cXhsVCjsLc%3D 10.1016/S1387-2656(04)10002-1 (Pubitemid 39419988)
    • (2004) Biotechnology Annual Review , vol.10 , Issue.SPEC. ISSUE , pp. 31-50
    • Cabrita, L.D.1    Bottomley, S.P.2
  • 22
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • DOI 10.1016/S0958-1669(98)80035-9
    • H Lilie E Schwarz R Rudolph 1998 Advances in refolding of proteins produced in E. coli Current Opinion in Biotechnology 9 497 501 10.1016/S0958-1669(98)80035-9 1:CAS:528:DyaK1cXntVSgtrk%3D 10.1016/S0958- 1669(98)80035-9 (Pubitemid 28478971)
    • (1998) Current Opinion in Biotechnology , vol.9 , Issue.5 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 23
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein folding
    • DOI 10.1016/S0076-6879(99)09017-5
    • E De Bernardez Clark E Schwarz R Rudolph 1999 Inhibition of aggregation side reactions during in vitro protein folding Methods in Enzymology 309 217 236 10.1016/S0076-6879(99)09017-5 10.1016/S0076-6879(99)09017-5 (Pubitemid 29446452)
    • (1999) Methods in Enzymology , vol.309 , pp. 217-236
    • De Bernardez Clark, E.1    Schwarz, E.2    Rudolph, R.3
  • 24
    • 67651158824 scopus 로고    scopus 로고
    • Role of oxidative stress in alcohol-induced liver injury
    • 10.1007/s00204-009-0432-0 1:CAS:528:DC%2BD1MXlvFyiu78%3D 10.1007/s00204-009-0432-0
    • AI Cederbaum Y Lu D Wu 2009 Role of oxidative stress in alcohol-induced liver injury Archives of Toxicology 83 519 548 10.1007/s00204-009-0432-0 1:CAS:528:DC%2BD1MXlvFyiu78%3D 10.1007/s00204-009-0432-0
    • (2009) Archives of Toxicology , vol.83 , pp. 519-548
    • Cederbaum, A.I.1    Lu, Y.2    Wu, D.3


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