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Volumn 57, Issue 2, 2008, Pages 244-254

Production and comprehensive quality control of recombinant human Interleukin-1β: A case study for a process development strategy

Author keywords

DAPase; Expression screening; His tag cleavage; Immobilized Metal Affinity Chromatography (IMAC); Interleukin 1 (IL 1 ); Ni NTA; Protein production; TAGZyme; X ray crystallography

Indexed keywords

DEOXYRIBONUCLEASE; ENDOTOXIN; EXOPEPTIDASE; HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; INTERLEUKIN 1BETA; OLIGOPEPTIDE; RECOMBINANT PROTEIN; RIBONUCLEASE; SERRATIA MARCESCENS NUCLEASE; UNCLASSIFIED DRUG;

EID: 37349073090     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2007.09.019     Document Type: Article
Times cited : (26)

References (64)
  • 1
    • 37349012594 scopus 로고    scopus 로고
    • Defining your product profile and maintaining control over it, Part 2, challenges of monitoring host cell protein impurities
    • Champion K., Madden H., Dougherty J., and Shacter E. Defining your product profile and maintaining control over it, Part 2, challenges of monitoring host cell protein impurities. BioProcess Int. (2005) 52-57
    • (2005) BioProcess Int. , pp. 52-57
    • Champion, K.1    Madden, H.2    Dougherty, J.3    Shacter, E.4
  • 2
    • 0034074086 scopus 로고    scopus 로고
    • Strategies for host cell protein analysis
    • Hoffman K. Strategies for host cell protein analysis. Biopharm 13 (2000) 38-45
    • (2000) Biopharm , vol.13 , pp. 38-45
    • Hoffman, K.1
  • 4
    • 37349028025 scopus 로고    scopus 로고
    • C. Lauritzen, G. Petersen, J. Pedersen, J. Arnau, U. Römer, F. Schäfer, Reliable, large-scale cleavage of tags from affinity-purified biopharmaceuticals, in: J. Knäblein, (Ed.), Modern Biopharmaceuticals-Recent success stories, Wiley-VCH, Weinheim, in press.
  • 5
    • 37349042244 scopus 로고    scopus 로고
    • A bit of advice on crystallizing proteins
    • Bergfors T.M. (Ed), International University Line, Biotechnology Series, La Jolla
    • McPherson A. A bit of advice on crystallizing proteins. In: Bergfors T.M. (Ed). Protein Crystallization-Techniques, Strategies, and Tips (1999), International University Line, Biotechnology Series, La Jolla 3-6
    • (1999) Protein Crystallization-Techniques, Strategies, and Tips , pp. 3-6
    • McPherson, A.1
  • 6
    • 4344698577 scopus 로고    scopus 로고
    • The use of recombinant methods and molecular engineering in protein crystallization
    • Derewenda Z.S. The use of recombinant methods and molecular engineering in protein crystallization. Methods 34 (2004) 354-363
    • (2004) Methods , vol.34 , pp. 354-363
    • Derewenda, Z.S.1
  • 7
    • 37349053478 scopus 로고    scopus 로고
    • Biocompare, protein chromatography: tools for protein expression and purification, Biocompare Suveys and Reports, Biocompare Inc., July 10, 2006.
  • 8
    • 0141539517 scopus 로고    scopus 로고
    • A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa
    • Jenny R.J., Mann K.G., and Lundblad R.L. A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa. Protein Expr. Purif. 31 (2003) 1-11
    • (2003) Protein Expr. Purif. , vol.31 , pp. 1-11
    • Jenny, R.J.1    Mann, K.G.2    Lundblad, R.L.3
  • 9
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • Arnau J., Lauritzen C., Petersen G.E., and Pedersen J. Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. Protein Expr. Purif. 48 (2006) 1-13
    • (2006) Protein Expr. Purif. , vol.48 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3    Pedersen, J.4
  • 10
    • 0033117468 scopus 로고    scopus 로고
    • Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases
    • Pedersen J., Lauritzen C., Thorup M.M., and Weis D.S. Removal of N-terminal polyhistidine tags from recombinant proteins using engineered aminopeptidases. Protein Expr. Purif. 15 (1999) 389-400
    • (1999) Protein Expr. Purif. , vol.15 , pp. 389-400
    • Pedersen, J.1    Lauritzen, C.2    Thorup, M.M.3    Weis, D.S.4
  • 11
    • 84867569623 scopus 로고    scopus 로고
    • A highly specific system for efficient enzymatic removal of tags from recombinant proteins
    • Schäfer F., Schäfer A., and Steinert K. A highly specific system for efficient enzymatic removal of tags from recombinant proteins. J. Biomolec. Techniques 13 (2002) 158-171
    • (2002) J. Biomolec. Techniques , vol.13 , pp. 158-171
    • Schäfer, F.1    Schäfer, A.2    Steinert, K.3
  • 12
    • 0032420423 scopus 로고    scopus 로고
    • Active recombinant rat dipeptidyl aminopeptidase I (cathepsin C) produced using the baculovirus expression system
    • Lauritzen C., Pedersen J., Madsen M.T., Justesen J., Martensen P.M., and Dahl S.W. Active recombinant rat dipeptidyl aminopeptidase I (cathepsin C) produced using the baculovirus expression system. Protein Expr. Purif. 14 (1998) 434-442
    • (1998) Protein Expr. Purif. , vol.14 , pp. 434-442
    • Lauritzen, C.1    Pedersen, J.2    Madsen, M.T.3    Justesen, J.4    Martensen, P.M.5    Dahl, S.W.6
  • 14
    • 0029877078 scopus 로고    scopus 로고
    • Interleukin 1 trials in cancer patients: a review of the toxicity, antitumor and hematopoietic effects
    • Veltri S., and Smith II J.W. Interleukin 1 trials in cancer patients: a review of the toxicity, antitumor and hematopoietic effects. Stem Cells 14 (1996) 164-176
    • (1996) Stem Cells , vol.14 , pp. 164-176
    • Veltri, S.1    Smith II, J.W.2
  • 16
    • 0031638712 scopus 로고    scopus 로고
    • Will adjuvants be needed for vaccines in the future?
    • Bomford R. Will adjuvants be needed for vaccines in the future?. Dev. Biol. Stand. 92 (1998) 13-17
    • (1998) Dev. Biol. Stand. , vol.92 , pp. 13-17
    • Bomford, R.1
  • 17
    • 1642346887 scopus 로고    scopus 로고
    • Expression in Escherichia coli and purification of sea bass (Dicentrarchus labrax) Interleukin 1β, a possible immunoadjuvant in aquaculture
    • Buonocore F., Mazzini M., Forlenza M., Randelli E., Secombes C.J., Zou J., and Scapigliatti G. Expression in Escherichia coli and purification of sea bass (Dicentrarchus labrax) Interleukin 1β, a possible immunoadjuvant in aquaculture. Mar. Biotechnol. 6 (2004) 53-59
    • (2004) Mar. Biotechnol. , vol.6 , pp. 53-59
    • Buonocore, F.1    Mazzini, M.2    Forlenza, M.3    Randelli, E.4    Secombes, C.J.5    Zou, J.6    Scapigliatti, G.7
  • 18
    • 0036140236 scopus 로고    scopus 로고
    • Cytokines as adjuvants for the induction of anti-human immunodeficiency virus peptide immunoglobulin G (IgG) and IgA antibodies in serum and mucosal secretions after nasal immunization
    • Bradney C.P., Sempowski G.D., Liao H.-X., Haynes B.F., and Staats H.F. Cytokines as adjuvants for the induction of anti-human immunodeficiency virus peptide immunoglobulin G (IgG) and IgA antibodies in serum and mucosal secretions after nasal immunization. J. Virol. 76 (2002) 517-524
    • (2002) J. Virol. , vol.76 , pp. 517-524
    • Bradney, C.P.1    Sempowski, G.D.2    Liao, H.-X.3    Haynes, B.F.4    Staats, H.F.5
  • 19
    • 0033562987 scopus 로고    scopus 로고
    • IL-1 is an effective adjuvant for mucosal and systemic immune response when coadministered with protein immunogens
    • Staats H.F., and Ennis Jr. F.A. IL-1 is an effective adjuvant for mucosal and systemic immune response when coadministered with protein immunogens. J. Immunol. 162 (1999) 6141-6147
    • (1999) J. Immunol. , vol.162 , pp. 6141-6147
    • Staats, H.F.1    Ennis Jr., F.A.2
  • 20
    • 0031569457 scopus 로고    scopus 로고
    • Cytokine-in-adjuvant steering of the immune response phenotype to Hiv-1 vaccine constructs - granulocyte-macrophage colony stimulating factor and Tnf-alpha synergize with IL-12 to enhance induction of cytotoxic T lymphocytes
    • Ahlers J.D., Dunlop N., Alling D.W., Nara P.L., and Berzofsky J.A. Cytokine-in-adjuvant steering of the immune response phenotype to Hiv-1 vaccine constructs - granulocyte-macrophage colony stimulating factor and Tnf-alpha synergize with IL-12 to enhance induction of cytotoxic T lymphocytes. J. Immunol. 158 (1997) 3947-3958
    • (1997) J. Immunol. , vol.158 , pp. 3947-3958
    • Ahlers, J.D.1    Dunlop, N.2    Alling, D.W.3    Nara, P.L.4    Berzofsky, J.A.5
  • 21
    • 0037513477 scopus 로고    scopus 로고
    • IL-1α, innate immunity, and skin carcinogenesis: the effect of consitutive expression of IL-1α in epidermis on chemical carcinogenesis
    • Murphy J.-E., Morales R.E., Scott J., and Kupper T.S. IL-1α, innate immunity, and skin carcinogenesis: the effect of consitutive expression of IL-1α in epidermis on chemical carcinogenesis. J. Immunol. 170 (2003) 5697-5703
    • (2003) J. Immunol. , vol.170 , pp. 5697-5703
    • Murphy, J.-E.1    Morales, R.E.2    Scott, J.3    Kupper, T.S.4
  • 22
    • 0034896456 scopus 로고    scopus 로고
    • Interleukin 2-antibody and Tumor Necrosis Factor-antibody fusion proteins induce different antitumor immune responses in vivo
    • Christ O., Matzku S., Burger C., and Zöller M. Interleukin 2-antibody and Tumor Necrosis Factor-antibody fusion proteins induce different antitumor immune responses in vivo. Clin. Cancer Res. 7 (2001) 1385-1397
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1385-1397
    • Christ, O.1    Matzku, S.2    Burger, C.3    Zöller, M.4
  • 23
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4, The CCP suite: Programs for protein crystallography, Acta Cryst. D 50 (1994) 760-763.
  • 25
    • 37349085850 scopus 로고    scopus 로고
    • note
    • Supplementary materials online (crystal picture, diffraction data, table with comprehensive IL-1β strutural data).
  • 26
    • 0032103808 scopus 로고    scopus 로고
    • Presence of an N-terminal polyhistidine tag facilitates stable expression of an otherwise unstable N-terminal domain of mouse tissue inhibitor of metalloproteinase-1 in Escherichia coli
    • Rajan S.S., Lackland H., Stein S., and Denhardt D.T. Presence of an N-terminal polyhistidine tag facilitates stable expression of an otherwise unstable N-terminal domain of mouse tissue inhibitor of metalloproteinase-1 in Escherichia coli. Protein Expr. Purif. 13 (1998) 67-72
    • (1998) Protein Expr. Purif. , vol.13 , pp. 67-72
    • Rajan, S.S.1    Lackland, H.2    Stein, S.3    Denhardt, D.T.4
  • 27
    • 23244467452 scopus 로고    scopus 로고
    • An improved strategy for high-level production of human vasostatin120-180
    • Sun Q.-M., Chen L.-L., Cao L., Fang L., Chen C., and Hua Z.-C. An improved strategy for high-level production of human vasostatin120-180. Biotechnol. Prog. 21 (2005) 1048-1052
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1048-1052
    • Sun, Q.-M.1    Chen, L.-L.2    Cao, L.3    Fang, L.4    Chen, C.5    Hua, Z.-C.6
  • 28
    • 0031466699 scopus 로고    scopus 로고
    • An efficient system for production of recombinant urokinase-type plasminogen activator
    • Tang W., Sun Z.-Y., Pannell R., Gurewich V., and Liu J.-N. An efficient system for production of recombinant urokinase-type plasminogen activator. Protein Expr. Purif. 11 (1997) 279-283
    • (1997) Protein Expr. Purif. , vol.11 , pp. 279-283
    • Tang, W.1    Sun, Z.-Y.2    Pannell, R.3    Gurewich, V.4    Liu, J.-N.5
  • 29
    • 33646882130 scopus 로고    scopus 로고
    • Histidine tag fusion increases expression levels of active recombinant amelogenin in Escherichia coli
    • Svensson J., Andersson C., Reseland J.E., Lyngstadaas P., and Bulow L. Histidine tag fusion increases expression levels of active recombinant amelogenin in Escherichia coli. Protein Expr. Purif. 48 (2006) 134-141
    • (2006) Protein Expr. Purif. , vol.48 , pp. 134-141
    • Svensson, J.1    Andersson, C.2    Reseland, J.E.3    Lyngstadaas, P.4    Bulow, L.5
  • 30
    • 31044446735 scopus 로고    scopus 로고
    • Rapid and easy thermodynamic optimization of the 5́end of mRNA dramatically increases the level of wild type protein expression in Escherichia coli
    • Cébe R., and Geiser M. Rapid and easy thermodynamic optimization of the 5́end of mRNA dramatically increases the level of wild type protein expression in Escherichia coli. Protein Expr. Purif. 45 (2006) 374-380
    • (2006) Protein Expr. Purif. , vol.45 , pp. 374-380
    • Cébe, R.1    Geiser, M.2
  • 31
    • 14644417891 scopus 로고    scopus 로고
    • Optimized expression of Plasmodium falciparum erythrocyte membrane protein I domains in Escherichia coli
    • Flick K., Ahuja S., Chene A., Bejarano MT., and Chen Q. Optimized expression of Plasmodium falciparum erythrocyte membrane protein I domains in Escherichia coli. Malaria J. 3 (2004) 50
    • (2004) Malaria J. , vol.3 , pp. 50
    • Flick, K.1    Ahuja, S.2    Chene, A.3    Bejarano, MT.4    Chen, Q.5
  • 32
    • 18844362113 scopus 로고    scopus 로고
    • Strategies for efficient production of heterologous proteins in Escherichia coli
    • Jana S., and Deb J.K. Strategies for efficient production of heterologous proteins in Escherichia coli. Appl. Microbiol. Biotechnol. 67 (2005) 289-298
    • (2005) Appl. Microbiol. Biotechnol. , vol.67 , pp. 289-298
    • Jana, S.1    Deb, J.K.2
  • 33
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier F.W. Protein production by auto-induction in high-density shaking cultures. Protein Expr. Purif. 41 (2005) 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 34
    • 3042587661 scopus 로고    scopus 로고
    • Increased peptide deformylase activity for N -formylmethionine processing of proteins overexpressed in Escherichia coli: application to homogenous rubredoxin production
    • Tang J., Hernandez G., and LeMaster D.M. Increased peptide deformylase activity for N -formylmethionine processing of proteins overexpressed in Escherichia coli: application to homogenous rubredoxin production. Protein Expr. Purif. 36 (2004) 100-105
    • (2004) Protein Expr. Purif. , vol.36 , pp. 100-105
    • Tang, J.1    Hernandez, G.2    LeMaster, D.M.3
  • 35
    • 0027482631 scopus 로고
    • A single cDNA, hTFIIA/α, encodes both the p35 and p19 subunits of human TFIIA
    • DeJong J., and Roeder R.G. A single cDNA, hTFIIA/α, encodes both the p35 and p19 subunits of human TFIIA. Genes Dev. 7 (1993) 2220-2234
    • (1993) Genes Dev. , vol.7 , pp. 2220-2234
    • DeJong, J.1    Roeder, R.G.2
  • 37
    • 33748578942 scopus 로고    scopus 로고
    • Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography
    • Bolanos-Garcia V.M., and Davies O.R. Structural analysis and classification of native proteins from E. coli commonly co-purified by immobilised metal affinity chromatography. Biochim. Biophys. Acta 1760 (2006) 1304-1313
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 1304-1313
    • Bolanos-Garcia, V.M.1    Davies, O.R.2
  • 38
    • 0035957867 scopus 로고    scopus 로고
    • Affinity chromatography of polyhistidine tagged enzymes: New dextran-coated immobilized metal ion affinity chromatography matrices for prevention of undesired multipoint adsorptions
    • Mateo C., Fernandez-Lorente G., Pessela B.C.C., Vian A., Carrascosa A.V., Garcia J.L., Fernandez-Lafuente R., and Guisan J.M. Affinity chromatography of polyhistidine tagged enzymes: New dextran-coated immobilized metal ion affinity chromatography matrices for prevention of undesired multipoint adsorptions. J. Chromatog. A 915 (2001) 97-106
    • (2001) J. Chromatog. A , vol.915 , pp. 97-106
    • Mateo, C.1    Fernandez-Lorente, G.2    Pessela, B.C.C.3    Vian, A.4    Carrascosa, A.V.5    Garcia, J.L.6    Fernandez-Lafuente, R.7    Guisan, J.M.8
  • 39
    • 0021077260 scopus 로고
    • Purification to homogeneity of pig leucocyte catabolin, a protein that causes cartilage resorption in vitro
    • Saklatvala J., Curry V.A., and Sarsfield S.J. Purification to homogeneity of pig leucocyte catabolin, a protein that causes cartilage resorption in vitro. Biochem. J. 215 (1983) 385-392
    • (1983) Biochem. J. , vol.215 , pp. 385-392
    • Saklatvala, J.1    Curry, V.A.2    Sarsfield, S.J.3
  • 41
    • 0023689282 scopus 로고
    • Resolution and biological properties of three N-terminal analogues of recombinant Interleukin-1β
    • Yem A.W., Richard K.A., Staite N.D., and Deibel Jr. M.R. Resolution and biological properties of three N-terminal analogues of recombinant Interleukin-1β. Lymphokine Res. 7 (1988) 85-92
    • (1988) Lymphokine Res. , vol.7 , pp. 85-92
    • Yem, A.W.1    Richard, K.A.2    Staite, N.D.3    Deibel Jr., M.R.4
  • 42
    • 0024380151 scopus 로고
    • Isolation and bioactivities of three IL-1β N-terminal variants
    • Richard K.A., Yem A.W., Deibel Jr. M.R., and Staite N.D. Isolation and bioactivities of three IL-1β N-terminal variants. Agents Actions 27 (1989) 268-270
    • (1989) Agents Actions , vol.27 , pp. 268-270
    • Richard, K.A.1    Yem, A.W.2    Deibel Jr., M.R.3    Staite, N.D.4
  • 43
    • 15744400080 scopus 로고    scopus 로고
    • Temperature, media, and point of induction affect the N-terminal processing of interleukin-1β
    • Covalt J.C., Cao T.B., Magdaroag J.R.C., Gross L.A., and Jennings P.A. Temperature, media, and point of induction affect the N-terminal processing of interleukin-1β. Prot. Expr. Purif. 41 (2005) 45-52
    • (2005) Prot. Expr. Purif. , vol.41 , pp. 45-52
    • Covalt, J.C.1    Cao, T.B.2    Magdaroag, J.R.C.3    Gross, L.A.4    Jennings, P.A.5
  • 46
    • 0028353230 scopus 로고
    • Production, purification and immunogenicity of a malaria-blocking vaccine candidate: TBV25H expressed in yeast and purified using Ni-NTA agarose
    • Kaslow D.C., and Shiloach J. Production, purification and immunogenicity of a malaria-blocking vaccine candidate: TBV25H expressed in yeast and purified using Ni-NTA agarose. Biotechnology 12 (1994) 494-499
    • (1994) Biotechnology , vol.12 , pp. 494-499
    • Kaslow, D.C.1    Shiloach, J.2
  • 47
    • 0002572930 scopus 로고    scopus 로고
    • Ni-NTA for large-scale processes-systematic investigation of separation characteristics, storage and CIP conditions, and leaching
    • Schäfer F., Blümer J., Römer U., and Steinert K. Ni-NTA for large-scale processes-systematic investigation of separation characteristics, storage and CIP conditions, and leaching. QIAGEN, QIAGEN News 4 (2000) 11-15
    • (2000) QIAGEN, QIAGEN News , vol.4 , pp. 11-15
    • Schäfer, F.1    Blümer, J.2    Römer, U.3    Steinert, K.4
  • 48
    • 0023781763 scopus 로고
    • Genetic approach to facilitate purification of recombinant proteins with a novel chelate adsorbent
    • Hochuli E., Bannwarth W., Döbeli H., Gentz R., and Stüber D. Genetic approach to facilitate purification of recombinant proteins with a novel chelate adsorbent. Biotechnology 6 (1988) 1321-1325
    • (1988) Biotechnology , vol.6 , pp. 1321-1325
    • Hochuli, E.1    Bannwarth, W.2    Döbeli, H.3    Gentz, R.4    Stüber, D.5
  • 49
    • 27144470222 scopus 로고    scopus 로고
    • Application of immobilized metal affinity chromatography in proteomics
    • Sun X., Chiu J.-F., and He Q.-Y. Application of immobilized metal affinity chromatography in proteomics. Expert Rev. Proteomics 2 (2005) 649-657
    • (2005) Expert Rev. Proteomics , vol.2 , pp. 649-657
    • Sun, X.1    Chiu, J.-F.2    He, Q.-Y.3
  • 50
    • 0032500509 scopus 로고    scopus 로고
    • + antiporter as well as the growth phenotype of Escherichia coli
    • + antiporter as well as the growth phenotype of Escherichia coli. J. Biol. Chem. 273 (1998) 26470-26476
    • (1998) J. Biol. Chem. , vol.273 , pp. 26470-26476
    • Rimon, A.1    Gerchmann, Y.2    Kariv, Z.3    Padan, E.4
  • 52
    • 0024997246 scopus 로고
    • Removal of endotoxion from protein solutions by phase separation using Triton X-114
    • Aida Y., and Pabst M.J. Removal of endotoxion from protein solutions by phase separation using Triton X-114. J. Immunol. Methods 132 (1990) 191-195
    • (1990) J. Immunol. Methods , vol.132 , pp. 191-195
    • Aida, Y.1    Pabst, M.J.2
  • 53
    • 33645409827 scopus 로고    scopus 로고
    • Single step protocol to purify recombinant proteins with low endotoxin contents
    • Reichelt P., Schwarz C., and Donzeau M. Single step protocol to purify recombinant proteins with low endotoxin contents. Protein Expr. Purif. 46 (2006) 483-488
    • (2006) Protein Expr. Purif. , vol.46 , pp. 483-488
    • Reichelt, P.1    Schwarz, C.2    Donzeau, M.3
  • 54
    • 33644687877 scopus 로고    scopus 로고
    • Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 Å
    • Du Z., Lee J.K., Tjhen R., Li S., Pan H., Stroud R., and James T.L. Crystal structure of the first KH domain of human poly(C)-binding protein-2 in complex with a C-rich strand of human telomeric DNA at 1.7 Å. J. Biol. Chem. 280 (2005) 28823-38830
    • (2005) J. Biol. Chem. , vol.280 , pp. 28823-38830
    • Du, Z.1    Lee, J.K.2    Tjhen, R.3    Li, S.4    Pan, H.5    Stroud, R.6    James, T.L.7
  • 55
    • 28944441962 scopus 로고    scopus 로고
    • Influence of the protein oligomericity on final yield after affinity tag removal in purification of recombinant proteins
    • Kenig M., Peternel S., Gaberc-Porekar V., and Menart V. Influence of the protein oligomericity on final yield after affinity tag removal in purification of recombinant proteins. J. Chromatogr. A 1101 (2006) 293-306
    • (2006) J. Chromatogr. A , vol.1101 , pp. 293-306
    • Kenig, M.1    Peternel, S.2    Gaberc-Porekar, V.3    Menart, V.4
  • 56
    • 0029823251 scopus 로고    scopus 로고
    • Increased production of peptide deformylase eliminates retention of formylmethionine in bovine somatotropin overproduced in Escherichia coli
    • Warren W.C., Bentle K.A., Schittler M.R., Schwane A.C., O'Neil J.P., and Bogosian G. Increased production of peptide deformylase eliminates retention of formylmethionine in bovine somatotropin overproduced in Escherichia coli. Gene 194 (1996) 235-238
    • (1996) Gene , vol.194 , pp. 235-238
    • Warren, W.C.1    Bentle, K.A.2    Schittler, M.R.3    Schwane, A.C.4    O'Neil, J.P.5    Bogosian, G.6
  • 58
    • 7044260891 scopus 로고    scopus 로고
    • Functional expression and characterization of a bacterial light-harvesting membrane protein in Escherichia coli and cell-free synthesis systems
    • Shimada Y., Wang Z.-Y., Mochizuki Y., Kobayashi M., and Nozawa T. Functional expression and characterization of a bacterial light-harvesting membrane protein in Escherichia coli and cell-free synthesis systems. Biosci. Biotechnol. Biochem. 68 (2004) 1942-1948
    • (2004) Biosci. Biotechnol. Biochem. , vol.68 , pp. 1942-1948
    • Shimada, Y.1    Wang, Z.-Y.2    Mochizuki, Y.3    Kobayashi, M.4    Nozawa, T.5
  • 59
    • 0033524454 scopus 로고    scopus 로고
    • Disordered water within a hydrophobic protein cavity visualized by X-ray crystallography
    • Yu B., Blaber M., Gronenburg A.M., Clore G.M., and Caspar D.L.D. Disordered water within a hydrophobic protein cavity visualized by X-ray crystallography. Proc. Natl. Acad. Sci. USA 96 (1999) 103-108
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 103-108
    • Yu, B.1    Blaber, M.2    Gronenburg, A.M.3    Clore, G.M.4    Caspar, D.L.D.5
  • 62
    • 37349035017 scopus 로고    scopus 로고
    • R.A. Young, Toxicity summary for nickel and nickel compounds, In: Risk assessment information systems-toxicity profiles, The Health and Sciences Research Division, Oak Ridge National Laboratories, Oak Ridge, Tennessee (1995), Available from: http://risk.lsd.ornl.gov/tox/profiles/nickel_and_nickel_compounds_c_V1.shtml.
  • 63
    • 37349055798 scopus 로고    scopus 로고
    • Food and Drug Administration, FDA, Guidance document for nickel in shellfish, Center for Food Safety and Applied Nutrition, CFSAN (1993), Available from: http://www.cfsan.fda.gov/∼frf/guid-ni.html.
  • 64
    • 37349046414 scopus 로고    scopus 로고
    • Food and Drug Administration, FDA, Total diet study, Center for Food Safety and Applied Nutrition, CFSAN (2007), Available from: http://www.cfsan.fda.gov/∼comm/tds-toc.html.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.