메뉴 건너뛰기




Volumn 82, Issue 5, 2003, Pages 605-611

One-step metal-affinity purification of histidine-tagged proteins by temperature-triggered precipitation

Author keywords

Elastin; His tag; Metal affinity; Protein purification

Indexed keywords

ALDEHYDES; PRECIPITATION (CHEMICAL); PURIFICATION; SYNTHESIS (CHEMICAL); THERMAL EFFECTS;

EID: 0037420917     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/bit.10609     Document Type: Article
Times cited : (51)

References (32)
  • 1
    • 0028108936 scopus 로고
    • Silica-based metal chelate affinity sorbents. II. Adsorption and elution behaviour of proteins on iminoacetic acid affinity sorbents prepared via different immobilization techniques
    • Anspach FB. 1994. Silica-based metal chelate affinity sorbents. II. Adsorption and elution behaviour of proteins on iminoacetic acid affinity sorbents prepared via different immobilization techniques. J Chromatogr A 676:249-266.
    • (1994) J Chromatogr A , vol.676 , pp. 249-266
    • Anspach, F.B.1
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0035809094 scopus 로고    scopus 로고
    • Variable specific activity of Escherichia coli β-galactosidase in bacterial cells
    • Cazorla D, Feliu JX, Villaverde A. 2001. Variable specific activity of Escherichia coli β-galactosidase in bacterial cells. Biotechnol Bioeng 72:255-260.
    • (2001) Biotechnol Bioeng , vol.72 , pp. 255-260
    • Cazorla, D.1    Feliu, J.X.2    Villaverde, A.3
  • 4
    • 0034737367 scopus 로고    scopus 로고
    • Immobilised metal affinity chromatography of β-galactosidase from unclarified Escherichia coli homogenates using expanded bed adsorption
    • Clemmitt RH, Chase HA. 2000. Immobilised metal affinity chromatography of β-galactosidase from unclarified Escherichia coli homogenates using expanded bed adsorption. J Chromatogr A 874:27-43.
    • (2000) J Chromatogr A , vol.874 , pp. 27-43
    • Clemmitt, R.H.1    Chase, H.A.2
  • 5
    • 0027604973 scopus 로고
    • Affinity thermoprecipitation: Contribution of the efficiency of ligand-protein interaction and access of the ligand
    • Galaev IY, Mattiasson B. 1993. Affinity thermoprecipitation: contribution of the efficiency of ligand-protein interaction and access of the ligand. Biotechnol Bioeng 41:1101-1106.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 1101-1106
    • Galaev, I.Y.1    Mattiasson, B.2
  • 6
    • 0242680019 scopus 로고    scopus 로고
    • Metal-copolymer complexes of N-isopropylacrylamide for affinity precipitation of proteins
    • Galaev IY, Kumar A, Mattiasson B. 1999. Metal-copolymer complexes of N-isopropylacrylamide for affinity precipitation of proteins. J.M.S.-Pure Appl Chem A36:1093-1105.
    • (1999) J.M.S.-Pure Appl Chem , vol.A36 , pp. 1093-1105
    • Galaev, I.Y.1    Kumar, A.2    Mattiasson, B.3
  • 8
    • 0023781763 scopus 로고
    • Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent
    • Hochuli E, Bannwarth W, Döbeli H, Gentz R, Stüber D. 1988. Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent. Bio/Technol 6:1321-1325.
    • (1988) Bio/Technol , vol.6 , pp. 1321-1325
    • Hochuli, E.1    Bannwarth, W.2    Döbeli, H.3    Gentz, R.4    Stüber, D.5
  • 9
    • 0029637138 scopus 로고
    • Multipoint binding and heterogenity in immobilized metal affinity chromatography
    • Johnson RD, Arnold FH. 1995. Multipoint binding and heterogenity in immobilized metal affinity chromatography. Biotechnol Bioeng 48:437-443.
    • (1995) Biotechnol Bioeng , vol.48 , pp. 437-443
    • Johnson, R.D.1    Arnold, F.H.2
  • 10
    • 0035957458 scopus 로고    scopus 로고
    • Tunable biopolymers for heavy metal removal
    • Kostal J, Mulchandani A, Chen W. 2001. Tunable biopolymers for heavy metal removal. Macromolecules 34:2257-2261.
    • (2001) Macromolecules , vol.34 , pp. 2257-2261
    • Kostal, J.1    Mulchandani, A.2    Chen, W.3
  • 11
    • 0032552491 scopus 로고    scopus 로고
    • Affinity precipitation of α-amylase inhibitors from wheat meal by metal chelate affinity binding using Cu(II)-loaded copolymers of 1-vinylimidazole with N-isopropylacrylamide
    • Kumar A, Galev IY, Mattiasson B. 1998. Affinity precipitation of α-amylase inhibitors from wheat meal by metal chelate affinity binding using Cu(II)-loaded copolymers of 1-vinylimidazole with N-isopropylacrylamide. Biotechnol Bioeng 59:695-704.
    • (1998) Biotechnol Bioeng , vol.59 , pp. 695-704
    • Kumar, A.1    Galev, I.Y.2    Mattiasson, B.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriofage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriofage T4. Nature 24:680-685.
    • (1970) Nature , vol.24 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 12944288256 scopus 로고    scopus 로고
    • High-resolution topographic imagining of environmentally responsive, elastinmimetic hydrogels
    • McMillan RA, Caran KL, Apkarian RP, Conticello VP. 1999. High-resolution topographic imagining of environmentally responsive, elastinmimetic hydrogels. Macromolecules 32:9067-9070.
    • (1999) Macromolecules , vol.32 , pp. 9067-9070
    • McMillan, R.A.1    Caran, K.L.2    Apkarian, R.P.3    Conticello, V.P.4
  • 15
    • 0030087535 scopus 로고    scopus 로고
    • Product purification by reversible phase transition following Escherichia coli expression of genes encoding up to 251 repeats of elastomeric pentapeptide GVGVG
    • McPherson DT, Xu J, Urry DW. 1996. Product purification by reversible phase transition following Escherichia coli expression of genes encoding up to 251 repeats of elastomeric pentapeptide GVGVG. Protein Expr Purif 7:51-57.
    • (1996) Protein Expr Purif , vol.7 , pp. 51-57
    • McPherson, D.T.1    Xu, J.2    Urry, D.W.3
  • 16
    • 0032739304 scopus 로고    scopus 로고
    • Purification of recombinant proteins by fusion with thermally-responsive polypeptides
    • Meyer DE, 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
  • 17
    • 0034878076 scopus 로고    scopus 로고
    • Protein purification by fusion with an environmentally responsive elastin-like polypeptide: Effect of polypeptide length on the purification of thioredoxin
    • Meyer DE, Trabbic-Carlson K, Chilkoti A. 2001. Protein purification by fusion with an environmentally responsive elastin-like polypeptide: effect of polypeptide length on the purification of thioredoxin. Biotechnol Prog 17:720-728.
    • (2001) Biotechnol Prog , vol.17 , pp. 720-728
    • Meyer, D.E.1    Trabbic-Carlson, K.2    Chilkoti, A.3
  • 23
    • 0242680018 scopus 로고    scopus 로고
    • Thermally triggered purification and immobilization of elastin-OPH fusions
    • Shimazu M, Mulchandani A, Chen W. 2003. Thermally triggered purification and immobilization of elastin-OPH fusions. Biotechnol Bioeng 81:74-79.
    • (2003) Biotechnol Bioeng , vol.81 , pp. 74-79
    • Shimazu, M.1    Mulchandani, A.2    Chen, W.3
  • 24
    • 0033621512 scopus 로고    scopus 로고
    • Applications of a peptide ligand for streptavidin: The Strep-tag
    • Skerra A, Schmidt TMG. 1999. Applications of a peptide ligand for streptavidin: the Strep-tag. Biomol Eng 16:79-86.
    • (1999) Biomol Eng , vol.16 , pp. 79-86
    • Skerra, A.1    Schmidt, T.M.G.2
  • 25
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutatione S-transferase
    • Smith DB, Johnson KS. 1988, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutatione S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 26
    • 0024296676 scopus 로고
    • Chelating peptideimmobilized metal ion affinity chromatography
    • Smith MC, Furman TC. Ingolia TD, Pidgeon C. 1988. Chelating peptideimmobilized metal ion affinity chromatography. J Biol Chem 263:7211-7215.
    • (1988) J Biol Chem , vol.263 , pp. 7211-7215
    • Smith, M.C.1    Furman, T.C.2    Ingolia, T.D.3    Pidgeon, C.4
  • 27
    • 0032520638 scopus 로고    scopus 로고
    • A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli
    • Smith PA, Tripp BC, DiBlasio-Smith EA, Lu Z, LaVallie ER, McCoy JM. 1998. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in Escherichia coli. Nucleic Acids Res 26:1414-1420.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1414-1420
    • Smith, P.A.1    Tripp, B.C.2    DiBlasio-Smith, E.A.3    Lu, Z.4    LaVallie, E.R.5    McCoy, J.M.6
  • 29
    • 0028157408 scopus 로고
    • Multiple-site binding interactions in metal-affinity chromatography
    • Todd RJ, Johnson RD, Arnold FH. 1994. Multiple-site binding interactions in metal-affinity chromatography. J Chromatogr A 662:13-26.
    • (1994) J Chromatogr A , vol.662 , pp. 13-26
    • Todd, R.J.1    Johnson, R.D.2    Arnold, F.H.3
  • 30
    • 0038388786 scopus 로고    scopus 로고
    • Physical chemistry of biological free energy transduction demonstrated by elastic protein-based polymers
    • Urry DW. 1997. Physical chemistry of biological free energy transduction demonstrated by elastic protein-based polymers. J Phys Chem B 101:11007-11028.
    • (1997) J Phys Chem B , vol.101 , pp. 11007-11028
    • Urry, D.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.