메뉴 건너뛰기




Volumn 284, Issue 1-2, 2004, Pages 165-175

Production of a biotinylated single-chain antibody fragment in the cytoplasm of Escherichia coli

Author keywords

Immunoassay; In vivo biotinylation; Oxidizing bacterial cytoplasm; scFv; Single chain antibody fragment expression

Indexed keywords

BIOTIN; CARRIER PROTEIN; HYBRID PROTEIN; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; THYROID STIMULATING IMMUNOGLOBULIN;

EID: 0347634531     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jim.2003.10.008     Document Type: Article
Times cited : (49)

References (39)
  • 2
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette P.H., Aslund F., Beckwith J., Georgiou G. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. U. S. A. 96:1999;13703.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13703
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 4
    • 0028108943 scopus 로고
    • Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase
    • Chapman-Smith A., Turner D.L., Cronan J.E. Jr., Morris T.W., Wallace J.C. Expression, biotinylation and purification of a biotin-domain peptide from the biotin carboxy carrier protein of Escherichia coli acetyl-CoA carboxylase. Biochem. J. 302:1994;881.
    • (1994) Biochem. J. , vol.302 , pp. 881
    • Chapman-Smith, A.1    Turner, D.L.2    Cronan, J.E.Jr.3    Morris, T.W.4    Wallace, J.C.5
  • 5
    • 0023679220 scopus 로고
    • Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination
    • Cronan J.E. Jr. Expression of the biotin biosynthetic operon of Escherichia coli is regulated by the rate of protein biotination. J. Biol. Chem. 263:1988;10332.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10332
    • Cronan, J.E.Jr.1
  • 6
    • 0025293361 scopus 로고
    • Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins
    • Cronan J.E. Jr. Biotination of proteins in vivo. A post-translational modification to label, purify, and study proteins. J. Biol. Chem. 265:1990;10327.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10327
    • Cronan, J.E.Jr.1
  • 7
    • 0025856887 scopus 로고
    • The biotin-(strept)avidin system: Principles and applications in biotechnology
    • Diamandis E.P., Christopoulos T.K. The biotin-(strept)avidin system: principles and applications in biotechnology. Clin. Chem. 37:1991;625.
    • (1991) Clin. Chem. , vol.37 , pp. 625
    • Diamandis, E.P.1    Christopoulos, T.K.2
  • 8
    • 0032505105 scopus 로고    scopus 로고
    • Site-specific, enzymatic biotinylation of recombinant proteins in Spodoptera frugiperda cells using biotin acceptor peptides
    • Duffy S., Tsao K.L., Waugh D.S. Site-specific, enzymatic biotinylation of recombinant proteins in Spodoptera frugiperda cells using biotin acceptor peptides. Anal. Biochem. 262:1998;122.
    • (1998) Anal. Biochem. , vol.262 , pp. 122
    • Duffy, S.1    Tsao, K.L.2    Waugh, D.S.3
  • 9
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert H.F. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63:1990;69.
    • (1990) Adv. Enzymol. Relat. Areas Mol. Biol. , vol.63 , pp. 69
    • Gilbert, H.F.1
  • 10
    • 0018721964 scopus 로고
    • The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
    • Goto Y., Hamaguchi K. The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain. J. Biochem. (Tokyo). 86:1979;1433.
    • (1979) J. Biochem. (Tokyo) , vol.86 , pp. 1433
    • Goto, Y.1    Hamaguchi, K.2
  • 12
    • 0013945155 scopus 로고
    • Optical rotatory dispersion, circular dichroism and far-ultraviolet spectra of avidin and streptavidin
    • Green N.M., Melamed M.D. Optical rotatory dispersion, circular dichroism and far-ultraviolet spectra of avidin and streptavidin. Biochem. J. 100:1966;614.
    • (1966) Biochem. J. , vol.100 , pp. 614
    • Green, N.M.1    Melamed, M.D.2
  • 15
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C., Sinskey A.J., Lodish H.F. Oxidized redox state of glutathione in the endoplasmic reticulum. Science. 257:1992;1496.
    • (1992) Science , vol.257 , pp. 1496
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 16
    • 0036296338 scopus 로고    scopus 로고
    • Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli
    • Jurado P., Ritz D., Beckwith J., de Lorenzo V., Fernandez L.A. Production of functional single-chain Fv antibodies in the cytoplasm of Escherichia coli. J. Mol. Biol. 320:2002;1.
    • (2002) J. Mol. Biol. , vol.320 , pp. 1
    • Jurado, P.1    Ritz, D.2    Beckwith, J.3    De Lorenzo, V.4    Fernandez, L.A.5
  • 17
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • Knappik A., Pluckthun A. Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng. 8:1995;81.
    • (1995) Protein Eng. , vol.8 , pp. 81
    • Knappik, A.1    Pluckthun, A.2
  • 18
    • 0031032155 scopus 로고    scopus 로고
    • Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system
    • Krebber A., Bornhauser S., Burmester J., Honegger A., Willuda J., Bosshard H.R., Pluckthun A. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J. Immunol. Methods. 201:1997;35.
    • (1997) J. Immunol. Methods , vol.201 , pp. 35
    • Krebber, A.1    Bornhauser, S.2    Burmester, J.3    Honegger, A.4    Willuda, J.5    Bosshard, H.R.6    Pluckthun, A.7
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 20
    • 0034756555 scopus 로고    scopus 로고
    • Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones
    • Levy R., Weiss R., Chen G., Iverson B.L., Georgiou G. Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones. Protein Expr. Purif. 23:2001;338.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 338
    • Levy, R.1    Weiss, R.2    Chen, G.3    Iverson, B.L.4    Georgiou, G.5
  • 21
    • 0026502763 scopus 로고
    • The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase
    • Li S.J., Cronan J.E. Jr. The gene encoding the biotin carboxylase subunit of Escherichia coli acetyl-CoA carboxylase. J. Biol. Chem. 267:1992;855.
    • (1992) J. Biol. Chem. , vol.267 , pp. 855
    • Li, S.J.1    Cronan, J.E.Jr.2
  • 23
    • 0033562345 scopus 로고    scopus 로고
    • Specific immobilization of in vivo biotinylated bacterial luciferase and FMN:NAD(P)H oxidoreductase
    • Min D.J., Andrade J.D., Stewart R.J. Specific immobilization of in vivo biotinylated bacterial luciferase and FMN:NAD(P)H oxidoreductase. Anal. Biochem. 270:1999;133.
    • (1999) Anal. Biochem. , vol.270 , pp. 133
    • Min, D.J.1    Andrade, J.D.2    Stewart, R.J.3
  • 24
    • 0029986466 scopus 로고    scopus 로고
    • Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase
    • Nenortas E., Beckett D. Purification and characterization of intact and truncated forms of the Escherichia coli biotin carboxyl carrier subunit of acetyl-CoA carboxylase. J. Biol. Chem. 271:1996;7559.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7559
    • Nenortas, E.1    Beckett, D.2
  • 25
    • 0026001727 scopus 로고
    • Escherichia coli exports previously folded and biotinated protein domains
    • Reed K.E., Cronan J.E. Jr. Escherichia coli exports previously folded and biotinated protein domains. J. Biol. Chem. 266:1991;11425.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11425
    • Reed, K.E.1    Cronan, J.E.Jr.2
  • 27
    • 0032212036 scopus 로고    scopus 로고
    • In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail
    • Saviranta P., Haavisto T., Rappu P., Karp M., Lovgren T. In vitro enzymatic biotinylation of recombinant fab fragments through a peptide acceptor tail. Bioconjug. Chem. 9:1998;725.
    • (1998) Bioconjug. Chem. , vol.9 , pp. 725
    • Saviranta, P.1    Haavisto, T.2    Rappu, P.3    Karp, M.4    Lovgren, T.5
  • 28
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz P.J. Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (NY). 11:1993;1138.
    • (1993) Biotechnology (NY) , vol.11 , pp. 1138
    • Schatz, P.J.1
  • 29
    • 0023939327 scopus 로고
    • Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii
    • Shenoy B.C., Wood H.G. Purification and properties of the synthetase catalyzing the biotination of the aposubunit of transcarboxylase from Propionibacterium shermanii. FASEB J. 2:1988;2396.
    • (1988) FASEB J. , vol.2 , pp. 2396
    • Shenoy, B.C.1    Wood, H.G.2
  • 30
    • 0032983924 scopus 로고    scopus 로고
    • In vivo biotinylated recombinant antibodies: High efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments
    • Sibler A.P., Kempf E., Glacet A., Orfanoudakis G., Bourel D., Weiss E. In vivo biotinylated recombinant antibodies: high efficiency of labelling and application to the cloning of active anti-human IgG1 Fab fragments. J. Immunol. Methods. 224:1999;129.
    • (1999) J. Immunol. Methods , vol.224 , pp. 129
    • Sibler, A.P.1    Kempf, E.2    Glacet, A.3    Orfanoudakis, G.4    Bourel, D.5    Weiss, E.6
  • 31
    • 0032520638 scopus 로고    scopus 로고
    • A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli
    • Smith P.A., Tripp B.C., DiBlasio-Smith E.A., Lu Z., LaVallie E.R., McCoy J.M. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Res. 26:1998;1414.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 1414
    • Smith, P.A.1    Tripp, B.C.2    Diblasio-Smith, E.A.3    Lu, Z.4    Lavallie, E.R.5    McCoy, J.M.6
  • 32
    • 0025753565 scopus 로고
    • Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli
    • Strandberg L., Enfors S.O. Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli. Appl. Environ. Microbiol. 57:1991;1669.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1669
    • Strandberg, L.1    Enfors, S.O.2
  • 33
    • 0029872080 scopus 로고    scopus 로고
    • A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli
    • Tsao K.L., DeBarbieri B., Michel H., Waugh D.S. A versatile plasmid expression vector for the production of biotinylated proteins by site-specific, enzymatic modification in Escherichia coli. Gene. 169:1996;59.
    • (1996) Gene , vol.169 , pp. 59
    • Tsao, K.L.1    Debarbieri, B.2    Michel, H.3    Waugh, D.S.4
  • 34
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker J., Grisshammer R. Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. J. 317:1996;891.
    • (1996) Biochem. J. , vol.317 , pp. 891
    • Tucker, J.1    Grisshammer, R.2
  • 35
    • 0036289146 scopus 로고    scopus 로고
    • High level production of functional antibody Fab fragments in an oxidizing bacterial cytoplasm
    • Venturi M., Seifert C., Hunte C. High level production of functional antibody Fab fragments in an oxidizing bacterial cytoplasm. J. Mol. Biol. 315:2002;1.
    • (2002) J. Mol. Biol. , vol.315 , pp. 1
    • Venturi, M.1    Seifert, C.2    Hunte, C.3
  • 36
    • 0025281379 scopus 로고
    • Introduction to avidin-biotin technology
    • Wilchek M., Bayer E.A. Introduction to avidin-biotin technology. Methods Enzymol. 184:1990;5.
    • (1990) Methods Enzymol. , vol.184 , pp. 5
    • Wilchek, M.1    Bayer, E.A.2
  • 39
    • 0021891877 scopus 로고
    • Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation
    • Ziegler D.M. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu. Rev. Biochem. Allied Res. India. 54:1985;305.
    • (1985) Annu. Rev. Biochem. Allied Res. India , vol.54 , pp. 305
    • Ziegler, D.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.