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Volumn , Issue SUPPL.58, 2009, Pages

Recombinant protein purification by unit 26.4 self-cleaving elastin-like polypeptide fusion tag

Author keywords

Elastin like polypeptide; Gateway cloning; Intein; Nonchromatographic bioseparations; Protein purification

Indexed keywords

AGAR; AMPICILLIN; BUFFER; DNA; ELASTIN; KANAMYCIN; POLYPEPTIDE; REAGENT; RECOMBINANT PROTEIN; ELASTIN LIKE POLYPEPTIDE; HYBRID PROTEIN; UNCLASSIFIED DRUG;

EID: 75749129871     PISSN: 19343655     EISSN: 19343663     Source Type: Journal    
DOI: 10.1002/0471140864.ps2604s58     Document Type: Review
Times cited : (9)

References (27)
  • 1
    • 24044491571 scopus 로고    scopus 로고
    • Simple bioseparations using self-cleaving elastinlike polypeptide tags
    • Banki, M.R., Feng, L., and Wood, D.W. 2005. Simple bioseparations using self-cleaving elastinlike polypeptide tags. Nat. Methods 2:659-661.
    • (2005) Nat. Methods , vol.2 , pp. 659-661
    • Banki, M.R.1    Feng, L.2    Wood, D.W.3
  • 2
    • 22444444258 scopus 로고    scopus 로고
    • Novel and economical purification of recombinant proteins: Intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association
    • Banki,M.R., Gerngross, U., andWood, D.W. 2005. Novel and economical purification of recombinant proteins: intein-mediated protein purification using in vivo polyhydroxybutyrate (PHB) matrix association. Protein Sci. 14:1387-1395.
    • (2005) Protein Sci. , vol.14 , pp. 1387-1395
    • Banki, M.R.1    Gerngross, U.2    Wood, D.W.3
  • 3
    • 28144460981 scopus 로고    scopus 로고
    • Inteins and affinity resin substitutes for protein purification and scale up
    • Banki, M.R. and Wood, D.W. 2005. Inteins and affinity resin substitutes for protein purification and scale up. Microb. Cell Fact 4:32.
    • (2005) Microb. Cell Fact , vol.4 , pp. 32
    • Banki, M.R.1    Wood, D.W.2
  • 4
    • 0022351236 scopus 로고
    • Control of directionality in lambda site specific recombination
    • Bushman, W., Thompson, J.F., Vargas, L., and Landy, A. 1985. Control of directionality in lambda site specific recombination. Science 230:906-911.
    • (1985) Science , vol.230 , pp. 906-911
    • Bushman, W.1    Thompson, J.F.2    Vargas, L.3    Landy, A.4
  • 6
    • 0032534048 scopus 로고    scopus 로고
    • Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step
    • Chong, S., Montello, G.E., Zhang, A., Cantor, E.J., Liao,W., Xu,M.Q., and Benner, J. 1998. Utilizing the C-terminal cleavage activity of a protein splicing element to purify recombinant proteins in a single chromatographic step. Nucleic Acids Res. 26:5109-5115.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5109-5115
    • Chong, S.1    Montello, G.E.2    Zhang, A.3    Cantor, E.J.4    Liao, W.5    Xu, M.Q.6    Benner, J.7
  • 7
    • 0026774103 scopus 로고
    • Protein splicing in the maturation of M. tuberculosis recA protein: A mechanism for tolerating a novel class of intervening sequence
    • Davis, E.O., Jenner, P.J., Brooks, P.C., Colston, M.J., and Sedgwick, S.G. 1992. Protein splicing in the maturation of M. tuberculosis recA protein: A mechanism for tolerating a novel class of intervening sequence. Cell 71:201-210.
    • (1992) Cell , vol.71 , pp. 201-210
    • Davis, E.O.1    Jenner, P.J.2    Brooks, P.C.3    Colston, M.J.4    Sedgwick, S.G.5
  • 8
    • 67349157562 scopus 로고    scopus 로고
    • Optimization of ELP-intein mediated protein purification by salt substitution
    • Fong, B.A.,Wu,W.Y., andWood, D.W. 2009. Optimization of ELP-intein mediated protein purification by salt substitution. Protein Expr. Purif. 66:198-202.
    • (2009) Protein Expr. Purif. , vol.66 , pp. 198-202
    • Fong, B.A.1    Wu, W.Y.2    Wood, D.W.3
  • 9
    • 23844438834 scopus 로고    scopus 로고
    • Selfcleavable stimulus responsive tags for protein purification without chromatography
    • Ge, X., Yang, D.S., Trabbic-Carlson, K., Kim, B., Chilkoti, A., and Filipe, C.D. 2005. Selfcleavable stimulus responsive tags for protein purification without chromatography. J. Am. Chem. Soc. 127:11228-11229.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11228-11229
    • Ge, X.1    Yang, D.S.2    Trabbic-Carlson, K.3    Kim, B.4    Chilkoti, A.5    Filipe, C.D.6
  • 10
    • 51649125516 scopus 로고    scopus 로고
    • Rapid cloning and purification of proteins: Gateway vectors for protein purification by self-cleaving tags
    • Gillies, A.R., Hsii, J.F., Oak, S., and Wood, D.W. 2008. Rapid cloning and purification of proteins: Gateway vectors for protein purification by self-cleaving tags. Biotechnol. Bioeng. 101:229-240.
    • (2008) Biotechnol. Bioeng. , vol.101 , pp. 229-240
    • Gillies, A.R.1    Hsii, J.F.2    Oak, S.3    Wood, D.W.4
  • 11
    • 28444477686 scopus 로고    scopus 로고
    • Minimization and stabilization of the Mycobacterium tuberculosis recA intein
    • Hiraga, K., Derbyshire, V., Dansereau, J.T., Van Roey, P., and Belfort, M. 2005. Minimization and stabilization of the Mycobacterium tuberculosis recA intein. J. Mol. Biol. 354:916-926.
    • (2005) J. Mol. Biol. , vol.354 , pp. 916-926
    • Hiraga, K.1    Derbyshire, V.2    Dansereau, J.T.3    Van Roey, P.4    Belfort, M.5
  • 12
    • 0034511180 scopus 로고    scopus 로고
    • Protein-splicing intein: Genetic mobility, origin, and evolution
    • Liu, X.Q. 2000. Protein-splicing intein: Genetic mobility, origin, and evolution. Annu. Rev. Genet. 34:61-76.
    • (2000) Annu. Rev. Genet. , vol.34 , pp. 61-76
    • Liu, X.Q.1
  • 13
    • 0026924813 scopus 로고
    • Hydrophobicity of amino acid residues: Differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin
    • Luan, C.H., Parker, T.M., Gowda, D.C., and Urry, D.W. 1992. Hydrophobicity of amino acid residues: Differential scanning calorimetry and synthesis of the aromatic analogues of the polypentapeptide of elastin. Biopolymers 32:1251-1261.
    • (1992) Biopolymers , vol.32 , pp. 1251-1261
    • Luan, C.H.1    Parker, T.M.2    Gowda, D.C.3    Urry, D.W.4
  • 14
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • Meyer, D.E. and Chilkoti, A. 1999. Purification of recombinant proteins by fusion with thermally-responsive polypeptides. Nat. Biotechnol. 17:1112-1115.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 1112-1115
    • Meyer, D.E.1    Chilkoti, A.2
  • 15
    • 2542628131 scopus 로고    scopus 로고
    • Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides
    • Meyer, D.E. and Chilkoti, A. 2004. Quantification of the effects of chain length and concentration on the thermal behavior of elastin-like polypeptides. Biomacromolecules 5:846-851.
    • (2004) Biomacromolecules , vol.5 , pp. 846-851
    • Meyer, D.E.1    Chilkoti, A.2
  • 16
    • 33947315594 scopus 로고    scopus 로고
    • Elastinlike polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves
    • Patel, J., Zhu, H., Menassa, R., Gyenis, L., Richman, A., and Brandle, J. 2007. Elastinlike polypeptide fusions enhance the accumulation of recombinant proteins in tobacco leaves. Transgenic Res. 16:239-249.
    • (2007) Transgenic Res. , vol.16 , pp. 239-249
    • Patel, J.1    Zhu, H.2    Menassa, R.3    Gyenis, L.4    Richman, A.5    Brandle, J.6
  • 18
    • 33847253510 scopus 로고    scopus 로고
    • Effect of NaCl on the exothermic and endothermic components of the inverse temperature transition of a model elastin-like polymer
    • Reguera, J., Urry, D.W., Parker, T.M., McPherson, D.T., and Rodriguez-Cabello, J.C. 2007. Effect of NaCl on the exothermic and endothermic components of the inverse temperature transition of a model elastin-like polymer. Biomacromolecules 8:354-358.
    • (2007) Biomacromolecules , vol.8 , pp. 354-358
    • Reguera, J.1    Urry, D.W.2    Parker, T.M.3    McPherson, D.T.4    Rodriguez-Cabello, J.C.5
  • 19
    • 0032988320 scopus 로고    scopus 로고
    • Purification of proteins fused to either the amino or carboxy terminus of the mycobacterium xenopi gyrase a intein
    • Southworth, M.W., Amaya, K., Evans, T.C., Xu, M.Q., and Perler, F.B. 1999. Purification of proteins fused to either the amino or carboxy terminus of the Mycobacterium xenopi gyrase A intein. Biotechniques 27:110-120.
    • (1999) Biotechniques , vol.27 , pp. 110-120
    • Southworth, M.W.1    Amaya, K.2    Evans, T.C.3    Xu, M.Q.4    Perler, F.B.5
  • 20
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • Terpe, K. 2003. Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems. Appl. Microbiol. Biotechnol. 60:523-533.
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 523-533
    • Terpe, K.1
  • 21
    • 9344234999 scopus 로고    scopus 로고
    • Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion
    • Trabbic-Carlson, K., Liu, L., Kim, B., and Chilkoti, A. 2004. Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion. Protein Sci. 13:3274-3284.
    • (2004) Protein Sci. , vol.13 , pp. 3274-3284
    • Trabbic-Carlson, K.1    Liu, L.2    Kim, B.3    Chilkoti, A.4
  • 22
    • 0023888219 scopus 로고
    • Entropic elastic processes in protein mechanisms. II. Simple (passive) and coupled (active) development of elastic forces
    • Urry, D.W. 1988. Entropic elastic processes in protein mechanisms. II. Simple (passive) and coupled (active) development of elastic forces. J. Protein Chem. 7:81-114.
    • (1988) J. Protein Chem. , vol.7 , pp. 81-114
    • Urry, D.W.1
  • 23
    • 33748232872 scopus 로고
    • Molecular machines: How motion and other functions of living organisms can result from reversible chemical changes
    • Urry, D.W. 1993. Molecular machines: How motion and other functions of living organisms can result from reversible chemical changes. Angewandte Chemie International Edition in English 32:819-841.
    • (1993) Angewandte Chemie International Edition in English , vol.32 , pp. 819-841
    • Urry, D.W.1
  • 25
    • 0022370012 scopus 로고
    • Phase-structure transitions of the elastin polypentapeptide-water system within the framework of composition-temperature studies
    • Urry, D.W., Trapane, T.L., and Prasad, K.U. 1985. Phase-structure transitions of the elastin polypentapeptide-water system within the framework of composition-temperature studies. Biopolymers 24:2345-2356.
    • (1985) Biopolymers , vol.24 , pp. 2345-2356
    • Urry, D.W.1    Trapane, T.L.2    Prasad, K.U.3
  • 26
    • 0034518359 scopus 로고    scopus 로고
    • Optimized single-step affinity purification with a selfcleaving intein applied to human acidic fibroblast growth factor
    • Wood, D.W., Derbyshire,V.,Wu,W., Chartrain, M., Belfort, M., and Belfort, G. 2000. Optimized single-step affinity purification with a selfcleaving intein applied to human acidic fibroblast growth factor. Biotechnol. Prog. 16:1055-1063.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 1055-1063
    • Derbyshirev., W.W.D.1    Wu, W.2    Chartrain, M.3    Belfort, M.4    Belfort, G.5
  • 27
    • 0032832776 scopus 로고    scopus 로고
    • A genetic system yields self-cleaving inteins for bioseparations
    • Wood, D.W., Wu, W., Belfort, G., Derbyshire, V., and Belfort, M. 1999. A genetic system yields self-cleaving inteins for bioseparations. Nat. Biotechnol. 17:889-892.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 889-892
    • Wood, D.W.1    Wu, W.2    Belfort, G.3    Derbyshire, V.4    Belfort, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.