메뉴 건너뛰기




Volumn 156, Issue 4, 2011, Pages 238-244

Cloning, expression, purification and characterization of a single chain variable fragment specific to tumor necrosis factor alpha in Escherichia coli

Author keywords

Cytotoxicity; Immobilized metal affinity chromatography (IMAC); Single chain variable fragment (ScFv); Soluble protein; Tumor necrosis factor (TNF )

Indexed keywords

AFFINITY CHROMATOGRAPHY; CYTOTOXICITY; DISEASES; ESCHERICHIA COLI; GLYCOPROTEINS; MACROPHAGES; METAL IONS; MOLECULES; MONOCLONAL ANTIBODIES; PURIFICATION; SUPPORT VECTOR MACHINES; TUMORS;

EID: 82955187801     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.06.039     Document Type: Article
Times cited : (21)

References (58)
  • 1
    • 4644309963 scopus 로고    scopus 로고
    • Production technologies for monoclonal antibodies and their fragments
    • Andersen D.C., Reilly D.E. Production technologies for monoclonal antibodies and their fragments. Curr. Opin. Biotechnol. 2004, 15:456-462.
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 456-462
    • Andersen, D.C.1    Reilly, D.E.2
  • 4
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 33847039612 scopus 로고    scopus 로고
    • Fast and efficient separation of immunoglobulin M from immunoglobulin G using short monolithic columns
    • Brne P., Podgornik A., Benčina K., Gabor B., Štrancar A., Peterka M. Fast and efficient separation of immunoglobulin M from immunoglobulin G using short monolithic columns. J. Chromatogr. A 2007, 1144(1):120-125.
    • (2007) J. Chromatogr. A , vol.1144 , Issue.1 , pp. 120-125
    • Brne, P.1    Podgornik, A.2    Benčina, K.3    Gabor, B.4    Štrancar, A.5    Peterka, M.6
  • 6
    • 0005382256 scopus 로고    scopus 로고
    • Restoration of transcriptional activity of p53 mutants in human tumour cells by intracellular expression of anti p53 single chain Fv fragments
    • Caron de Fromentel C., Gruel N., Venot C., Debussche L., Conseiller E., Dureuil C., Teillaud J.L., Tocque B., Bracco L. Restoration of transcriptional activity of p53 mutants in human tumour cells by intracellular expression of anti p53 single chain Fv fragments. Oncogene 1999, 18:551-557.
    • (1999) Oncogene , vol.18 , pp. 551-557
    • Caron de Fromentel, C.1    Gruel, N.2    Venot, C.3    Debussche, L.4    Conseiller, E.5    Dureuil, C.6    Teillaud, J.L.7    Tocque, B.8    Bracco, L.9
  • 7
    • 0028836167 scopus 로고
    • Purification of bacterially expressed single chain Fv antibodies for clinical applications using metal chelate chromatography
    • Casey J.L., Keep P.A., Chester K.A., Robson L., Hawkins R.E., Begen R.H.J. Purification of bacterially expressed single chain Fv antibodies for clinical applications using metal chelate chromatography. J. Immunol. Methods 1995, 179:105-116.
    • (1995) J. Immunol. Methods , vol.179 , pp. 105-116
    • Casey, J.L.1    Keep, P.A.2    Chester, K.A.3    Robson, L.4    Hawkins, R.E.5    Begen, R.H.J.6
  • 8
    • 33746713752 scopus 로고    scopus 로고
    • Anti TNF-α and Th1 cytokine directed therapies for the treatment of asthma
    • Cazzola M., Polosa R. Anti TNF-α and Th1 cytokine directed therapies for the treatment of asthma. Curr. Opin. Allergy Clin. Immunol. 2006, 6:43-50.
    • (2006) Curr. Opin. Allergy Clin. Immunol. , vol.6 , pp. 43-50
    • Cazzola, M.1    Polosa, R.2
  • 10
    • 13244278838 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of single-chain variable fragment antibody against mycotoxin deoxynivalenol in recombinant Escherichia coli
    • Choi G.H., Lee D.H., Min W.K., Cho Y.J., Kweon D.H., Son D.H., Park K., Seo J.H. Cloning, expression, and characterization of single-chain variable fragment antibody against mycotoxin deoxynivalenol in recombinant Escherichia coli. Protein Expr. Purif. 2005, 35:84-92.
    • (2005) Protein Expr. Purif. , vol.35 , pp. 84-92
    • Choi, G.H.1    Lee, D.H.2    Min, W.K.3    Cho, Y.J.4    Kweon, D.H.5    Son, D.H.6    Park, K.7    Seo, J.H.8
  • 11
    • 0026808537 scopus 로고
    • Construction, characterization, and mutagenesis of an anti fluorescein single chain antibody idiotype family
    • Denzin L.K., Voss E.W. Construction, characterization, and mutagenesis of an anti fluorescein single chain antibody idiotype family. J. Biol. Chem. 1992, 267:8925-8931.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8925-8931
    • Denzin, L.K.1    Voss, E.W.2
  • 12
    • 0028136310 scopus 로고
    • Multimerization behavior of single chain Fv variants for the tumour-binding antibody B72.3
    • Desplancq D., King D.J., Lawson A.D.G., Mountain A. Multimerization behavior of single chain Fv variants for the tumour-binding antibody B72.3. Protein Eng. 1994, 7:1027-1033.
    • (1994) Protein Eng. , vol.7 , pp. 1027-1033
    • Desplancq, D.1    King, D.J.2    Lawson, A.D.G.3    Mountain, A.4
  • 14
    • 0026900343 scopus 로고
    • Regulated secretion and purification of recombinant antibodies in E. coli
    • Dübel S., Breitling F., Klewinghaus I., Little M. Regulated secretion and purification of recombinant antibodies in E. coli. Cell Biophys. 1992, 21:69-79.
    • (1992) Cell Biophys. , vol.21 , pp. 69-79
    • Dübel, S.1    Breitling, F.2    Klewinghaus, I.3    Little, M.4
  • 15
    • 79953321383 scopus 로고    scopus 로고
    • Monoliths for the purification of whey protein-dextran conjugates
    • Etzel M.R., Bund T. Monoliths for the purification of whey protein-dextran conjugates. J. Chromatogr. A 2011, 1218:2445-2450.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 2445-2450
    • Etzel, M.R.1    Bund, T.2
  • 16
    • 0030912095 scopus 로고    scopus 로고
    • Identification of framework residues in a secreted recombinant antibody fragment that control production level and localization in E. coli
    • Forstberg G., Forsgren M., Jaki M., Norin M., Sterky C., Enhörning A., Larsson K., Ericsson M., Björk P. Identification of framework residues in a secreted recombinant antibody fragment that control production level and localization in E. coli. J. Biol. Chem. 1997, 272:12430-12436.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12430-12436
    • Forstberg, G.1    Forsgren, M.2    Jaki, M.3    Norin, M.4    Sterky, C.5    Enhörning, A.6    Larsson, K.7    Ericsson, M.8    Björk, P.9
  • 17
    • 37249088464 scopus 로고    scopus 로고
    • Overexpression, effective renaturation, and bioactivity of novel single-chain antibodies against TNF-α
    • Geng S., Chang H., Qin W., Li Y., Feng J., Shen B. Overexpression, effective renaturation, and bioactivity of novel single-chain antibodies against TNF-α. Prep. Biochem. Biotechnol. 2008, 38:74-86.
    • (2008) Prep. Biochem. Biotechnol. , vol.38 , pp. 74-86
    • Geng, S.1    Chang, H.2    Qin, W.3    Li, Y.4    Feng, J.5    Shen, B.6
  • 18
    • 0030236157 scopus 로고    scopus 로고
    • ErbB-2 knockout employing an intracellular single-chain antibody (ScFv) accomplishes specific toxicity in erbB-2-expressing lung cancer cells
    • Grim J., Deshane J., Feng M., Lieber A., Kay M., Curiel D.T. erbB-2 knockout employing an intracellular single-chain antibody (ScFv) accomplishes specific toxicity in erbB-2-expressing lung cancer cells. Am. J. Respir. Cell Mol. Biol. 1996, 15:348-354.
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.15 , pp. 348-354
    • Grim, J.1    Deshane, J.2    Feng, M.3    Lieber, A.4    Kay, M.5    Curiel, D.T.6
  • 19
    • 0030669223 scopus 로고    scopus 로고
    • A single chain Fv fragment of P-glycoprotein-specific monoclonal antibody C219. Design, expression and crystal structure at 2.4Å resolution
    • Hoedemaeker F.J., Signorelli T., Johns K., Kuntz D.A., Rose D.R. A single chain Fv fragment of P-glycoprotein-specific monoclonal antibody C219. Design, expression and crystal structure at 2.4Å resolution. J. Biol. Chem. 1997, 272:29784-29789.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29784-29789
    • Hoedemaeker, F.J.1    Signorelli, T.2    Johns, K.3    Kuntz, D.A.4    Rose, D.R.5
  • 20
    • 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
  • 21
    • 0004198722 scopus 로고
    • Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli
    • Huston J.S., Levinson D., Mudgett-Hunter M., Tai M.S., Novotny J., Margolies M.N. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl. Acad. Sci. 1988, 85:5879-5883.
    • (1988) Proc. Natl. Acad. Sci. , vol.85 , pp. 5879-5883
    • Huston, J.S.1    Levinson, D.2    Mudgett-Hunter, M.3    Tai, M.S.4    Novotny, J.5    Margolies, M.N.6
  • 22
    • 13844280981 scopus 로고    scopus 로고
    • Application of two types of CIM tube column for purification of microbial enzymes
    • Isobe K., Kawakami Y. Application of two types of CIM tube column for purification of microbial enzymes. J. Chromatogr. A 2005, 1065:129-134.
    • (2005) J. Chromatogr. A , vol.1065 , pp. 129-134
    • Isobe, K.1    Kawakami, Y.2
  • 23
    • 0142232284 scopus 로고    scopus 로고
    • The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi
    • Joosten V., Lokman C., Van Den Hondel C.A., Punt P.J. The production of antibody fragments and antibody fusion proteins by yeasts and filamentous fungi. Microb. Cell Fact. 2003, 2:1-3.
    • (2003) Microb. Cell Fact. , vol.2 , pp. 1-3
    • Joosten, V.1    Lokman, C.2    Van Den Hondel, C.A.3    Punt, P.J.4
  • 24
    • 0035836059 scopus 로고    scopus 로고
    • Monoliths as stationary phases for separation of proteins and polynucleotides and enzymatic conversion
    • Josic D., Buchacher A., Jungbauer A. Monoliths as stationary phases for separation of proteins and polynucleotides and enzymatic conversion. J. Chromatogr. B 2001, 752(2):191-205.
    • (2001) J. Chromatogr. B , vol.752 , Issue.2 , pp. 191-205
    • Josic, D.1    Buchacher, A.2    Jungbauer, A.3
  • 25
    • 65249137637 scopus 로고    scopus 로고
    • Golimumab, a new human tumor necrosis factor alpha antibody, administered every four weeks as a subcutaneous injection in psoriatic arthritis: twenty-four-week efficacy and safety results of a randomized, placebo-controlled study
    • Kavanaugh A., McInnes I., Mease P., Krueger G.G., Gladman D., Gomez-Reino J., Papp K., Zrubek J., Mudivarthy S., Mack M., Visvanathan S., Beutler A. Golimumab, a new human tumor necrosis factor alpha antibody, administered every four weeks as a subcutaneous injection in psoriatic arthritis: twenty-four-week efficacy and safety results of a randomized, placebo-controlled study. Arthritis Rheum. 2009, 60:976-986.
    • (2009) Arthritis Rheum. , vol.60 , pp. 976-986
    • Kavanaugh, A.1    McInnes, I.2    Mease, P.3    Krueger, G.G.4    Gladman, D.5    Gomez-Reino, J.6    Papp, K.7    Zrubek, J.8    Mudivarthy, S.9    Mack, M.10    Visvanathan, S.11    Beutler, A.12
  • 27
    • 0032813516 scopus 로고    scopus 로고
    • On the role of tumor necrosis factor and receptors in models of multi organ failure, rheumatoid arthritis, multiple sclerosis and inflammatory bowel disease
    • Kollias G., Douni E., Kassiotis G., Kontoyiannis D. On the role of tumor necrosis factor and receptors in models of multi organ failure, rheumatoid arthritis, multiple sclerosis and inflammatory bowel disease. Immunol. Rev. 1999, 169:175-194.
    • (1999) Immunol. Rev. , vol.169 , pp. 175-194
    • Kollias, G.1    Douni, E.2    Kassiotis, G.3    Kontoyiannis, D.4
  • 28
    • 0014949207 scopus 로고
    • Cleavage of a structural protein during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of a structural protein during the assembly of the head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 3242724293 scopus 로고    scopus 로고
    • Expression and purification of a recombinant ScFv towards the exotoxin of the pathogen, Burkholderia pseudomallei
    • Lim K.P., Li H., Nathan S. Expression and purification of a recombinant ScFv towards the exotoxin of the pathogen, Burkholderia pseudomallei. J. Microbiol. 2004, 42:126-132.
    • (2004) J. Microbiol. , vol.42 , pp. 126-132
    • Lim, K.P.1    Li, H.2    Nathan, S.3
  • 31
    • 49249090889 scopus 로고    scopus 로고
    • A novel bivalent single-chain variable fragment (ScFv) inhibits the action of tumour necrosis factor alpha
    • Liu M., Wang X., Yin C., Zhang Z., Lin Q., Zhen Y., Huang H. A novel bivalent single-chain variable fragment (ScFv) inhibits the action of tumour necrosis factor alpha. Biotechnol. Appl. Biochem. 2008, 50:173-179.
    • (2008) Biotechnol. Appl. Biochem. , vol.50 , pp. 173-179
    • Liu, M.1    Wang, X.2    Yin, C.3    Zhang, Z.4    Lin, Q.5    Zhen, Y.6    Huang, H.7
  • 32
    • 24044485278 scopus 로고    scopus 로고
    • Cloning, expression, purification, and characterization of LC-1 ScFv with GFP tag
    • Lu M., Gong X.G., Yu H., Li J.Y. Cloning, expression, purification, and characterization of LC-1 ScFv with GFP tag. J. Zhejiang Univ. Sci. 2005, 6B8:832-837.
    • (2005) J. Zhejiang Univ. Sci. , pp. 832-837
    • Lu, M.1    Gong, X.G.2    Yu, H.3    Li, J.Y.4
  • 33
    • 0029863393 scopus 로고    scopus 로고
    • Comparative properties of the single chain antibody and Fv derivatives of mAb 4-4-20
    • Mallender W.D., Carrero J., Voss E.W. Comparative properties of the single chain antibody and Fv derivatives of mAb 4-4-20. J. Biol. Chem. 1996, 271:5338-5346.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5338-5346
    • Mallender, W.D.1    Carrero, J.2    Voss, E.W.3
  • 34
    • 0033524159 scopus 로고    scopus 로고
    • Infliximab (chimeric anti-tumor necrosis factor α monoclonal antibody) versus placebo in rheumatoid arthritis patients receiving concomitant methotrexate: a randomized phase III trial
    • Maini R., Clair E.W.St., Breedveld F., Frust D., Kalden J., Weisman M., Smolen J., Emery P., Harriman G., Feldmann M. Infliximab (chimeric anti-tumor necrosis factor α monoclonal antibody) versus placebo in rheumatoid arthritis patients receiving concomitant methotrexate: a randomized phase III trial. Lancet 1999, 354:1932-1939.
    • (1999) Lancet , vol.354 , pp. 1932-1939
    • Maini, R.1    Clair, E.2    Breedveld, F.3    Frust, D.4    Kalden, J.5    Weisman, M.6    Smolen, J.7    Emery, P.8    Harriman, G.9    Feldmann, M.10
  • 35
    • 0027299755 scopus 로고
    • TNF-alpha in rheumatoid arthritis and prospects of anti TNF therapy
    • Maini R.N., Brennan F.M., Williams R. TNF-alpha in rheumatoid arthritis and prospects of anti TNF therapy. Clin. Exp. Rheumatol. 1993, 11:173-175.
    • (1993) Clin. Exp. Rheumatol. , vol.11 , pp. 173-175
    • Maini, R.N.1    Brennan, F.M.2    Williams, R.3
  • 36
    • 0033032935 scopus 로고    scopus 로고
    • Cell-free expression of two single-chain monoclonal antibodies against lysozyme: effect of domain arrangement on the expression
    • Merk H., Stiege W., Tsumoto K., Kumagai I., Erdmann V.A. Cell-free expression of two single-chain monoclonal antibodies against lysozyme: effect of domain arrangement on the expression. J. Biochem. 1999, 125:328-333.
    • (1999) J. Biochem. , vol.125 , pp. 328-333
    • Merk, H.1    Stiege, W.2    Tsumoto, K.3    Kumagai, I.4    Erdmann, V.A.5
  • 37
    • 22244486057 scopus 로고    scopus 로고
    • Production, purification, and characterization of human ScFv antibodies expressed in Saccharomyces cerevisiae, Pichia pastoris, and Escherichia coli
    • Miller K.D., Weaver-Feldhaus J., Gray S.A., Siegel R.W., Feldhaus M.J. Production, purification, and characterization of human ScFv antibodies expressed in Saccharomyces cerevisiae, Pichia pastoris, and Escherichia coli. Protein Expr. Purif. 2005, 42:255-267.
    • (2005) Protein Expr. Purif. , vol.42 , pp. 255-267
    • Miller, K.D.1    Weaver-Feldhaus, J.2    Gray, S.A.3    Siegel, R.W.4    Feldhaus, M.J.5
  • 38
    • 78650936661 scopus 로고    scopus 로고
    • Isolation and purification of blood group antigens using immuno-affinity chromatography on short monolithic columns
    • Mönstera A., Hiller O., Grügerb D., Blasczykb R., Kaspera C. Isolation and purification of blood group antigens using immuno-affinity chromatography on short monolithic columns. J. Chromatogr. A 2011, 1218:706-710.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 706-710
    • Mönstera, A.1    Hiller, O.2    Grügerb, D.3    Blasczykb, R.4    Kaspera, C.5
  • 42
    • 0021114727 scopus 로고
    • Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials: serum protein affinities for gel-immobilized iron and nickel ions
    • Porath J., Olin B. Immobilized metal ion affinity adsorption and immobilized metal ion affinity chromatography of biomaterials: serum protein affinities for gel-immobilized iron and nickel ions. Biochemistry 1983, 22:1621-1630.
    • (1983) Biochemistry , vol.22 , pp. 1621-1630
    • Porath, J.1    Olin, B.2
  • 43
    • 0034726409 scopus 로고    scopus 로고
    • Synthesis of high avidity antibody fragments for cancer imaging
    • Power B.E., Hudson P.J. Synthesis of high avidity antibody fragments for cancer imaging. J. Immunol. Methods 2000, 242:193-204.
    • (2000) J. Immunol. Methods , vol.242 , pp. 193-204
    • Power, B.E.1    Hudson, P.J.2
  • 44
    • 77952668608 scopus 로고    scopus 로고
    • Characterization of metal chelate methacrylate monolithic disk for purification of polyclonal and monoclonal immunoglobulin G
    • Prasanna R.R., Vijayalakshmi M.A. Characterization of metal chelate methacrylate monolithic disk for purification of polyclonal and monoclonal immunoglobulin G. J. Chromatogr. A 2010, 1217(23):3660-3667.
    • (2010) J. Chromatogr. A , vol.1217 , Issue.23 , pp. 3660-3667
    • Prasanna, R.R.1    Vijayalakshmi, M.A.2
  • 45
    • 0025801974 scopus 로고
    • Purification of anti-epithelical mucin monoclonal antibodies by epitope affinity chromatography
    • Price M.R., Sekowski M., Tendler S.J.B. Purification of anti-epithelical mucin monoclonal antibodies by epitope affinity chromatography. J. Immunol. Methods 1991, 139:83-90.
    • (1991) J. Immunol. Methods , vol.139 , pp. 83-90
    • Price, M.R.1    Sekowski, M.2    Tendler, S.J.B.3
  • 46
    • 0029114769 scopus 로고
    • Intracellular antibodies: development and therapeutic potential
    • Richardson J.H., Marasco W.A. Intracellular antibodies: development and therapeutic potential. Trends Biotechnol. 1995, 13:306-310.
    • (1995) Trends Biotechnol. , vol.13 , pp. 306-310
    • Richardson, J.H.1    Marasco, W.A.2
  • 47
    • 0031766998 scopus 로고    scopus 로고
    • Prokaryotic expression of ScFv antibodies: secretion in L-form cells of Proteus mirabilis leads to active and overcomes the limitations of periplasmic expression in E. coli
    • Rippmann J.F., Klein M., Hoischen C., Brocks B., Rettig W.J., Gumpert J., Pfizenmaier K., Mattes R., Moosmayer D. Prokaryotic expression of ScFv antibodies: secretion in L-form cells of Proteus mirabilis leads to active and overcomes the limitations of periplasmic expression in E. coli. Appl. Environ. Microbiol. 1998, 64:4862-4869.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4862-4869
    • Rippmann, J.F.1    Klein, M.2    Hoischen, C.3    Brocks, B.4    Rettig, W.J.5    Gumpert, J.6    Pfizenmaier, K.7    Mattes, R.8    Moosmayer, D.9
  • 48
    • 0032803526 scopus 로고    scopus 로고
    • Synthesis, cloning & expression of single-chain Fv gene of the Hpr specific monoclonal antibody, Jel 42. Determination of binding constants with wild-type and mutant HPrs
    • Smallshaw J.E., Georges F., Lee J.S., Waygood E.B. Synthesis, cloning & expression of single-chain Fv gene of the Hpr specific monoclonal antibody, Jel 42. Determination of binding constants with wild-type and mutant HPrs. Protein Eng. 1999, 12:623-630.
    • (1999) Protein Eng. , vol.12 , pp. 623-630
    • Smallshaw, J.E.1    Georges, F.2    Lee, J.S.3    Waygood, E.B.4
  • 49
    • 0024671191 scopus 로고
    • The saga of IMAC and MIT
    • Sulkowski E. The saga of IMAC and MIT. Bioessays 1989, 10:170-175.
    • (1989) Bioessays , vol.10 , pp. 170-175
    • Sulkowski, E.1
  • 51
    • 0033974045 scopus 로고    scopus 로고
    • An introduction to monolithic disks as stationary phases for high performance biochromatography
    • Tennikova T.B., Freitag R. An introduction to monolithic disks as stationary phases for high performance biochromatography. J. High Resolut. Chromatogr. 2000, 23:27-38.
    • (2000) J. High Resolut. Chromatogr. , vol.23 , pp. 27-38
    • Tennikova, T.B.1    Freitag, R.2
  • 52
    • 0027199724 scopus 로고
    • High-performance membrane chromatography: highly efficient separation method for proteins in ion-exchange, hydrophobic interaction and reversed-phase modes
    • Tennikova T.B., Svec F. High-performance membrane chromatography: highly efficient separation method for proteins in ion-exchange, hydrophobic interaction and reversed-phase modes. J. Chromatogr. 1993, 646:279-288.
    • (1993) J. Chromatogr. , vol.646 , pp. 279-288
    • Tennikova, T.B.1    Svec, F.2
  • 53
    • 3242756761 scopus 로고    scopus 로고
    • Immobilized metal-ion affinity chromatography of human antibodies and their proteolytic fragments
    • Todorova-Balvay D., Pitiot O., Bourhim M., Srikrishnan T., Vijayalakshmi M. Immobilized metal-ion affinity chromatography of human antibodies and their proteolytic fragments. J. Chromatogr. B 2004, 808(1):57-62.
    • (2004) J. Chromatogr. B , vol.808 , Issue.1 , pp. 57-62
    • Todorova-Balvay, D.1    Pitiot, O.2    Bourhim, M.3    Srikrishnan, T.4    Vijayalakshmi, M.5
  • 54
    • 77951687530 scopus 로고    scopus 로고
    • Construction and characterization of a novel fusion protein MG7-ScFv/SEB against gastric cancer
    • Tong Q., Liu K., Lu X.M., Shu X.G., Wang G.B. Construction and characterization of a novel fusion protein MG7-ScFv/SEB against gastric cancer. J. Biomed. Biotechnol. 2010, 121094-121102.
    • (2010) J. Biomed. Biotechnol. , pp. 121094-121102
    • Tong, Q.1    Liu, K.2    Lu, X.M.3    Shu, X.G.4    Wang, G.B.5
  • 55
    • 0037049890 scopus 로고    scopus 로고
    • IMAC of human IgG: studies with IDA-immobilized copper, nickel, zinc, and cobalt ions and different buffer systems
    • Vancan S., Miranda E.A., Bueno S.M.A. IMAC of human IgG: studies with IDA-immobilized copper, nickel, zinc, and cobalt ions and different buffer systems. Process Biochem. 2002, 37(6):573-579.
    • (2002) Process Biochem. , vol.37 , Issue.6 , pp. 573-579
    • Vancan, S.1    Miranda, E.A.2    Bueno, S.M.A.3
  • 56
    • 38349122119 scopus 로고    scopus 로고
    • Expression, purification, and characterization of an immunotoxin containing a humanized anti-CD25 single chain fragment variable antibody fused to a modified truncated Pseudomonas exotoxin A
    • Wang H., Dai J., Li B., Fan K., Peng L., Zhang D. Expression, purification, and characterization of an immunotoxin containing a humanized anti-CD25 single chain fragment variable antibody fused to a modified truncated Pseudomonas exotoxin A. Protein Expr. Purif. 2008, 58:140-147.
    • (2008) Protein Expr. Purif. , vol.58 , pp. 140-147
    • Wang, H.1    Dai, J.2    Li, B.3    Fan, K.4    Peng, L.5    Zhang, D.6
  • 58
    • 0026684815 scopus 로고
    • Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms
    • Yokota T., Milenic D., Whitlow M., Schlom J. Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res. 1992, 52:19923402-19923408.
    • (1992) Cancer Res. , vol.52 , pp. 19923402-19923408
    • Yokota, T.1    Milenic, D.2    Whitlow, M.3    Schlom, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.