메뉴 건너뛰기




Volumn 75, Issue 1, 2011, Pages 75-82

A new tagged-TEV protease: Construction, optimisation of production, purification and test activity

Author keywords

Affinity chromatography; High level of production; Solubility; Streptag II TEV

Indexed keywords

HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; HYBRID PROTEIN; OLIGOPEPTIDE; PROTEINASE; TEV PROTEASE; VIRUS PROTEIN;

EID: 78049317940     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.08.012     Document Type: Article
Times cited : (28)

References (33)
  • 2
    • 30944459888 scopus 로고    scopus 로고
    • Improved solubility of TEV protease by direct evolution
    • S.V.D. Berg, P.. Löfdahl, T. Härd, and H. Berglund Improved solubility of TEV protease by direct evolution J. Biotechnol. 121 2006 291 298
    • (2006) J. Biotechnol. , vol.121 , pp. 291-298
    • Berg, S.V.D.1    Löfdahl, P.2    Härd, T.3    Berglund, H.4
  • 4
    • 15244363693 scopus 로고    scopus 로고
    • Self-cleavage of fusion protein in vivo using TEV protease to yield native protein
    • Y.P. Shih, H.C. Wu, S.M. Hu, T.F. Wang, and A.H.J. Wang Self-cleavage of fusion protein in vivo using TEV protease to yield native protein Protein Sci. 14 2005 936 941
    • (2005) Protein Sci. , vol.14 , pp. 936-941
    • Shih, Y.P.1    Wu, H.C.2    Hu, S.M.3    Wang, T.F.4    Wang, A.H.J.5
  • 5
    • 0013091910 scopus 로고    scopus 로고
    • Inhibition of tobacco etch virus protease activity by detergents
    • A.K. Mohanty, C.R. Simmons, and M.C. Wiener Inhibition of tobacco etch virus protease activity by detergents Protein Express. Purif. 27 2003 109 114
    • (2003) Protein Express. Purif. , vol.27 , pp. 109-114
    • Mohanty, A.K.1    Simmons, C.R.2    Wiener, M.C.3
  • 6
    • 33751408438 scopus 로고    scopus 로고
    • An improved strategy for high-level production of TEV protease in Escherichia coli and its purification and characterization
    • L. Fang, K.Z. Jia, Y.L. Tang, D.Y. Ma, M. Yu, and Z.C. Hua An improved strategy for high-level production of TEV protease in Escherichia coli and its purification and characterization Protein Express. Purif. 51 2007 102 109
    • (2007) Protein Express. Purif. , vol.51 , pp. 102-109
    • Fang, L.1    Jia, K.Z.2    Tang, Y.L.3    Ma, D.Y.4    Yu, M.5    Hua, Z.C.6
  • 7
    • 0035095521 scopus 로고    scopus 로고
    • Large-scale purification of a stable form of recombinant tobacco etch virus protease
    • L.J. Lucast, R.T. Batey, and J.A. Doudna Large-scale purification of a stable form of recombinant tobacco etch virus protease Biotechniques 30 2001 544 554
    • (2001) Biotechniques , vol.30 , pp. 544-554
    • Lucast, L.J.1    Batey, R.T.2    Doudna, J.A.3
  • 8
    • 34250348569 scopus 로고    scopus 로고
    • A combined approach to improving large-scale production of tobacco etch virus protease
    • P.G. Blommel, and B.G. Fox A combined approach to improving large-scale production of tobacco etch virus protease Protein Express. Purif. 55 2007 53 68
    • (2007) Protein Express. Purif. , vol.55 , pp. 53-68
    • Blommel, P.G.1    Fox, B.G.2
  • 9
    • 0029989229 scopus 로고    scopus 로고
    • Expression of correctly folded proteins in Escherichia coli
    • G. Georgiou, and P. Valax Expression of correctly folded proteins in Escherichia coli Curr. Opin. Biotechnol. 7 1996 190 197
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 190-197
    • Georgiou, G.1    Valax, P.2
  • 10
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • D.S. Waugh Making the most of affinity tags Trends Biotechnol. 23 2005 316 320
    • (2005) Trends Biotechnol. , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 11
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • R.B. Kapust, and D.S. Waugh Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci. 8 1999 1668 1674
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 12
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-tag and streptavidin for recombinant protein purification and detection
    • A. Skerra, and T.G.M. Schmidt Use of the Strep-tag and streptavidin for recombinant protein purification and detection Methods Enzymol. 326 2000 271 304
    • (2000) Methods Enzymol. , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.G.M.2
  • 13
    • 33847128295 scopus 로고    scopus 로고
    • Use of dual affinity tags for expression and purification of functional peripheral cannabinoid receptor
    • A. Yeliseev, L. Zoubak, and K. Gawrisch Use of dual affinity tags for expression and purification of functional peripheral cannabinoid receptor Protein Express. Purif. 53 2007 153 163
    • (2007) Protein Express. Purif. , vol.53 , pp. 153-163
    • Yeliseev, A.1    Zoubak, L.2    Gawrisch, K.3
  • 14
    • 13844266546 scopus 로고    scopus 로고
    • Purification of recombinant proteins from mammalian cell culture using a generic double-affinity chromatography scheme
    • B. Cass, P.L. Pham, A. Kamen, and Y. Durocher Purification of recombinant proteins from mammalian cell culture using a generic double-affinity chromatography scheme Protein Express. Purif. 40 2005 77 85
    • (2005) Protein Express. Purif. , vol.40 , pp. 77-85
    • Cass, B.1    Pham, P.L.2    Kamen, A.3    Durocher, Y.4
  • 15
    • 0027499708 scopus 로고
    • The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment
    • T.G.M. Schmidt, and A. Skerra The random peptide library-assisted engineering of a C-terminal affinity peptide, useful for the detection and purification of a functional Ig Fv fragment Protein Eng. 6 1993 109 122
    • (1993) Protein Eng. , vol.6 , pp. 109-122
    • Schmidt, T.G.M.1    Skerra, A.2
  • 16
    • 0036129945 scopus 로고    scopus 로고
    • Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site
    • I.P. Korndörfer, and A. Skerra Improved affinity of engineered streptavidin for the Strep-tag II peptide is due to a fixed open conformation of the lid-like loop at the binding site Protein Sci. 11 2002 883 893
    • (2002) Protein Sci. , vol.11 , pp. 883-893
    • Korndörfer, I.P.1    Skerra, A.2
  • 17
    • 0032524072 scopus 로고    scopus 로고
    • Strep-tag II affinity purification: An approach to study intermediates of metalloenzyme biosynthesis
    • T. Maier, N. Drapal, M. Thanbichler, and A. Böck Strep-tag II affinity purification: an approach to study intermediates of metalloenzyme biosynthesis Anal. Biochem. 259 1998 68 73
    • (1998) Anal. Biochem. , vol.259 , pp. 68-73
    • Maier, T.1    Drapal, N.2    Thanbichler, M.3    Böck, A.4
  • 18
    • 0029865819 scopus 로고    scopus 로고
    • Molecular interactions between the Strep-tag affinity peptide and its cognate target, streptavidin
    • T.G.M. Schmidt, J. Koepke, R. Frank, and A. Skerra Molecular interactions between the Strep-tag affinity peptide and its cognate target, streptavidin J. Mol. Biol. 255 1996 753 766
    • (1996) J. Mol. Biol. , vol.255 , pp. 753-766
    • Schmidt, T.G.M.1    Koepke, J.2    Frank, R.3    Skerra, A.4
  • 19
    • 0035543198 scopus 로고    scopus 로고
    • One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-tag
    • A.D. Keefe, D.S. Wilson, B. Seelig, and J.W. Szostak One-step purification of recombinant proteins using a nanomolar-affinity streptavidin-binding peptide, the SBP-tag Protein Express. Purif. 23 2001 440 446
    • (2001) Protein Express. Purif. , vol.23 , pp. 440-446
    • Keefe, A.D.1    Wilson, D.S.2    Seelig, B.3    Szostak, J.W.4
  • 20
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • T.G.M. Schmidt, and A. Skerra The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins Nat. Protocol 2 2007 1528 1535
    • (2007) Nat. Protocol , vol.2 , pp. 1528-1535
    • Schmidt, T.G.M.1    Skerra, A.2
  • 21
    • 0030780364 scopus 로고    scopus 로고
    • Mutagenesis of a flexible loop in streptavidin leads to higher affinity for the Strep-tag II peptide and improved performance in recombinant protein purification
    • S. Voss, and A. Skerra Mutagenesis of a flexible loop in streptavidin leads to higher affinity for the Strep-tag II peptide and improved performance in recombinant protein purification Protein Eng. 10 1997 975 982
    • (1997) Protein Eng. , vol.10 , pp. 975-982
    • Voss, S.1    Skerra, A.2
  • 22
    • 0029000550 scopus 로고
    • Expression and purification of a recombinant tobacco etch virus NIa proteinase: Biochemical analyses of the full-length and a naturally occurring truncated proteinase form
    • D. Parks, E.D. Howard, T.J. Wolpert, D.J. Arp, and W.G. Dougherty Expression and purification of a recombinant tobacco etch virus NIa proteinase: biochemical analyses of the full-length and a naturally occurring truncated proteinase form Virology 210 1995 194 201
    • (1995) Virology , vol.210 , pp. 194-201
    • Parks, D.1    Howard, E.D.2    Wolpert, T.J.3    Arp, D.J.4    Dougherty, W.G.5
  • 24
    • 0037434442 scopus 로고    scopus 로고
    • Evaluation of different promoters and host strains for the high-level expression of collagen-like polymer in Escherichia coli
    • J. Yin, J.H. Lin, W.T. Li, and D.I.C. Wang Evaluation of different promoters and host strains for the high-level expression of collagen-like polymer in Escherichia coli J. Biotechnol. 100 2003 181 191
    • (2003) J. Biotechnol. , vol.100 , pp. 181-191
    • Yin, J.1    Lin, J.H.2    Li, W.T.3    Wang, D.I.C.4
  • 25
    • 51049099424 scopus 로고    scopus 로고
    • Comparisons of recombinant protein expression in diverse natural isolates of Escherichia coli
    • Y. Jung, and D. Lim Comparisons of recombinant protein expression in diverse natural isolates of Escherichia coli Mol. Cells 25 2008 446 451
    • (2008) Mol. Cells , vol.25 , pp. 446-451
    • Jung, Y.1    Lim, D.2
  • 26
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • H.P. Sørensen, and K.K. Mortensen Advanced genetic strategies for recombinant protein expression in Escherichia coli J. Biotechnol. 115 2005 113 128
    • (2005) J. Biotechnol. , vol.115 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 28
    • 0032726773 scopus 로고    scopus 로고
    • One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex i by means of Strep-tag affinity chromatography
    • S. Bungert, B. Krafft, R. Schlesinger, and T. Friedrich One-step purification of the NADH dehydrogenase fragment of the Escherichia coli complex I by means of Strep-tag affinity chromatography FEBS Lett. 460 1999 207 211
    • (1999) FEBS Lett. , vol.460 , pp. 207-211
    • Bungert, S.1    Krafft, B.2    Schlesinger, R.3    Friedrich, T.4
  • 29
    • 33747666218 scopus 로고    scopus 로고
    • Overview of bacterial expression systems for heterologous protein production: From molecular and biochemical fundamentals to commercial systems
    • K. Terpe Overview of bacterial expression systems for heterologous protein production: from molecular and biochemical fundamentals to commercial systems Appl. Microbiol. Biotechnol. 72 2006 211 222
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 211-222
    • Terpe, K.1
  • 30
    • 0032588635 scopus 로고    scopus 로고
    • Strep-tag II for one-step affinity purification of active bHLH-zip domain of human c-Myc
    • N. Zwicker, K. Adelhelm, R. Thiericke, S. Grabley, and F. Hanel Strep-tag II for one-step affinity purification of active bHLH-zip domain of human c-Myc Biotechniques 27 1999 368 375
    • (1999) Biotechniques , vol.27 , pp. 368-375
    • Zwicker, N.1    Adelhelm, K.2    Thiericke, R.3    Grabley, S.4    Hanel, F.5
  • 31
    • 0034888426 scopus 로고    scopus 로고
    • Construction, overexpression, and purification of Arthrobacter globiformis amine oxidase-Strep-tag II fusion protein
    • G.A. Juda, J.A. Bollinger, and D.M. Dooley Construction, overexpression, and purification of Arthrobacter globiformis amine oxidase-Strep-tag II fusion protein Protein Express. Purif. 22 2001 455 461
    • (2001) Protein Express. Purif. , vol.22 , pp. 455-461
    • Juda, G.A.1    Bollinger, J.A.2    Dooley, D.M.3
  • 33
    • 0035711194 scopus 로고    scopus 로고
    • Tobacco etch virus protease: Mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency
    • R.B. Kapust, J. Tözsér, J.D. Fox, D.E. Anderson, S. Cherry, T.D. Copland, and D.S. Waugh Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency Protein Eng. 14 2001 993 1000
    • (2001) Protein Eng. , vol.14 , pp. 993-1000
    • Kapust, R.B.1    Tözsér, J.2    Fox, J.D.3    Anderson, D.E.4    Cherry, S.5    Copland, T.D.6    Waugh, D.S.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.