메뉴 건너뛰기




Volumn 26, Issue 2, 2002, Pages 301-308

Rapid refolding and polishing of single-chain antibodies from Escherichia coli inclusion bodies

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI;

EID: 0036425175     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00538-7     Document Type: Article
Times cited : (26)

References (21)
  • 1
    • 0034726409 scopus 로고    scopus 로고
    • Synthesis of high avidity antibody fragments (scFv multimers) for cancer imaging
    • B.E. Power, P.J. Hudson, Synthesis of high avidity antibody fragments (scFv multimers) for cancer imaging, J. Immunol. Methods 242 (1-2) (2000) 193-204.
    • (2000) J. Immunol. Methods , vol.242 , Issue.1-2 , pp. 193-204
    • Power, B.E.1    Hudson, P.J.2
  • 2
    • 0034283815 scopus 로고    scopus 로고
    • Noninvasive localization of tumors by immunofluorescence imaging using a single chain Fv fragment of a human monoclonal antibody with broad cancer specificity
    • B. Ramjiawan, P. Maiti, A. Aftanas, H. Kaplan, D. Fast, H.H. Mantsch, M. Jackson, Noninvasive localization of tumors by immunofluorescence imaging using a single chain Fv fragment of a human monoclonal antibody with broad cancer specificity, Cancer 89 (5) (2001) 1134-1144.
    • (2001) Cancer , vol.89 , Issue.5 , pp. 1134-1144
    • Ramjiawan, B.1    Maiti, P.2    Aftanas, A.3    Kaplan, H.4    Fast, D.5    Mantsch, H.H.6    Jackson, M.7
  • 4
    • 0029931209 scopus 로고    scopus 로고
    • Affinity maturation of recombinant antibodies using E. coli mutator cells
    • R.A. Irving, A.A. Kortt, P.J. Hudson, APnity maturation of recombinant antibodies using E. coli mutator cells, Immunotech-nology 2 (2) (1996) 127-143.
    • (1996) Immunotechnology , vol.2 , Issue.2 , pp. 127-143
    • Irving, R.A.1    Kortt, A.A.2    Hudson, P.J.3
  • 5
    • 0011261417 scopus 로고    scopus 로고
    • Challenges in scale-up of antibody production
    • McKenna, Challenges in scale-up of antibody production, Genet. Eng. News 21 (14) (2001) 10.
    • (2001) Genet. Eng. News , vol.21 , Issue.14 , pp. 10
    • McKenna1
  • 6
    • 0032122306 scopus 로고    scopus 로고
    • Antibody engineering: Comparison of bacterial yeast insect and mammalian expression systems
    • R. Verma, E. Boleti, A.J.T. George, Antibody engineering: Comparison of bacterial yeast insect and mammalian expression systems, J. Immunol. Methods 216 (1-2) (1998) 165-181
    • (1998) J. Immunol. Methods , vol.216 , Issue.1-2 , pp. 165-181
    • Verma, R.1    Boleti, E.2    George, A.J.T.3
  • 8
    • 0028361545 scopus 로고
    • Anti-metatype antibodies stabilize the fluorescein single-chain antibody 4-4-20 complex against dissociation by hydrostatic pressure
    • T. Coelho-Sampaio, E.W. Voss Jr., Anti-metatype antibodies stabilize the fluorescein single-chain antibody 4-4-20 complex against dissociation by hydrostatic pressure, J. Biol. Chem. 269 (11) (1994) 8146-8152.
    • (1994) J. Biol. Chem. , vol.269 , Issue.11 , pp. 8146-8152
    • Coelho-Sampaio, T.1    Voss E.W., Jr.2
  • 9
    • 0028046701 scopus 로고
    • High resolution structures of the 4-4-20 Fab fluorescein complex in two solvent systems-effects of solvent on structure and antigen binding affinity
    • J.N. Herron, A.H. Terry, S. Johnston, X.M. He, L.W. Guddat, E.W. Voss Jr., A.B. Edmundson, High resolution structures of the 4-4-20 Fab fluorescein complex in two solvent systems-effects of solvent on structure and antigen binding affinity, Biophys. J. 67 (6) (1994) 2167-2183.
    • (1994) Biophys. J. , vol.67 , Issue.6 , pp. 2167-2183
    • Herron, J.N.1    Terry, A.H.2    Johnston, S.3    He, X.M.4    Guddat, L.W.5    Voss E.W., Jr.6    Edmundson, A.B.7
  • 10
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment
    • L. Nieba, A. Honegger, C. Krebber, A. Pluckthun, Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment, Protein Eng. 10 (4) (1997) 435-444.
    • (1997) Protein Eng. , vol.10 , Issue.4 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Pluckthun, A.4
  • 12
    • 0024537949 scopus 로고
    • Comparison of variable region primary structures within an anti-fluorescein idiotype family
    • W.D. Bedzyk, L.S. Johnson, G.S. Riordan, E.W. Voss Jr., Comparison of variable region primary structures within an anti-fluorescein idiotype family, J. Biol. Chem. 264 (3) (1989) 1565-1569.
    • (1989) J. Biol. Chem. , vol.264 , Issue.3 , pp. 1565-1569
    • Bedzyk, W.D.1    Johnson, L.S.2    Riordan, G.S.3    Voss E.W., Jr.4
  • 13
    • 0034718615 scopus 로고    scopus 로고
    • Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
    • E.T. Boder, K.S. Midelfort, K.D. Wittrup, Directed evolution of antibody fragments with monovalent femtomolar antigen-binding aPnity, Proc. Natl. Acad. Sci. USA 97 (20) (2000) 10701-10705
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , Issue.20 , pp. 10701-10705
    • Boder, E.T.1    Midelfort, K.S.2    Wittrup, K.D.3
  • 15
    • 0001932972 scopus 로고
    • Single-chain Fv design and production by preparative folding
    • C.A.K. Borrebaeck (Ed.), Oxford University Press, New York
    • Huston et al., Single-chain Fv design and production by preparative folding, in: C.A.K. Borrebaeck (Ed.), Antibody Engineering, Oxford University Press, New York, 1995, pp. 185-227.
    • (1995) Antibody Engineering , pp. 185-227
    • Huston1
  • 16
    • 0032191701 scopus 로고    scopus 로고
    • Highly efficient recovery of functional single chain FV fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - Application to a human single-chain Fv fragment
    • K. Tsumoto, K. Shinoki, H. Kondo, M. Uchikawa, T. Juji, I. Kumagai, Highly efficient recovery of functional single chain FV fragments from inclusion bodies overexpressed in Escherichia coli by controlled introduction of oxidizing reagent - Application to a human single-chain Fv fragment, J. Immunol. Methods 219 (1-2) (1998) 119-129.
    • (1998) J. Immunol. Methods , vol.219 , Issue.1-2 , pp. 119-129
    • Tsumoto, K.1    Shinoki, K.2    Kondo, H.3    Uchikawa, M.4    Juji, T.5    Kumagai, I.6
  • 17
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • R.S. Sikorski, P. Hieter, A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharo-myces cerevisiae, Genetics 122 (1) (1989) 19-27.
    • (1989) Genetics , vol.122 , Issue.1 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 19
    • 0345195967 scopus 로고    scopus 로고
    • Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment
    • K.M. Arndt, K.M. Muller, A. Pluckthun, Factors influencing the dimer to monomer transition of an antibody single-chain Fv fragment, Biochemistry 37 (37) (1998) 12918-12926.
    • (1998) Biochemistry , vol.37 , Issue.37 , pp. 12918-12926
    • Arndt, K.M.1    Muller, K.M.2    Pluckthun, A.3
  • 20
    • 0031660079 scopus 로고    scopus 로고
    • Contributions of a highly conserved Vh/Vl hydrogen bonding interaction to scFv folding stability and refolding efficiency
    • P.H. Tan, B.M. Sandmaier, P.S. Stayton, Contributions of a highly conserved Vh/Vl hydrogen bonding interaction to scFv folding stability and refolding efficiency, Biophys. J. 75 (3) (1998) 1473-1482.
    • (1998) Biophys. J. , vol.75 , Issue.3 , pp. 1473-1482
    • Tan, P.H.1    Sandmaier, B.M.2    Stayton, P.S.3
  • 21
    • 0032703669 scopus 로고    scopus 로고
    • Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying
    • J.M. Sarciaux, S. Mansour, M.J. Hageman, S.L. Nail, Effects of buffer composition and processing conditions on aggregation of bovine IgG during freeze-drying, J. Pharm. Sci. 88 (12) (1999) 1354-1361.
    • (1999) J. Pharm. Sci. , vol.88 , Issue.12 , pp. 1354-1361
    • Sarciaux, J.M.1    Mansour, S.2    Hageman, M.J.3    Nail, S.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.