메뉴 건너뛰기




Volumn 79, Issue 2, 2011, Pages 191-196

Strategy for improvement of enteropeptidase efficiency in tag removal processes

Author keywords

Enteropeptidase; Enzyme specificity; Recombinant fusion proteins; Tag removal

Indexed keywords

ARGININE; ENTEROPEPTIDASE; FIBROBLAST GROWTH FACTOR 2; HYBRID PROTEIN; LYSINE; OLIGOPEPTIDE; THIOREDOXIN; TRYPSINOGEN; TUMOR NECROSIS FACTOR RELATED APOPTOSIS INDUCING LIGAND;

EID: 80051582702     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.04.005     Document Type: Article
Times cited : (23)

References (26)
  • 1
    • 0037255597 scopus 로고    scopus 로고
    • Overview of tag protein fusions: From molecular and biochemical fundamentals to commercial systems
    • K. Terpe Overview of tag protein fusions: from molecular and biochemical fundamentals to commercial systems Appl. Microbiol. Biotechnol. 60 2003 523 533 (Pubitemid 36169526)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.5 , pp. 523-533
    • Terpe, K.1
  • 2
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • DOI 10.1016/j.copbio.2006.06.003, PII S0958166906000875
    • D. Esposito, and D.K. Chatterjee Enhancement of soluble protein expression through the use of fusion tags Curr. Opin. Biotechnol. 17 2006 353 358 (Pubitemid 44163452)
    • (2006) Current Opinion in Biotechnology , vol.17 , Issue.4 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 3
    • 33646857665 scopus 로고    scopus 로고
    • Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins
    • DOI 10.1016/j.pep.2005.12.002, PII S1046592805004262
    • J. Arnau, C. Lauritzen, G.E. Petersen, and J. Pedersen Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins Protein Expr. Purif. 48 2006 1 13 (Pubitemid 43782626)
    • (2006) Protein Expression and Purification , vol.48 , Issue.1 , pp. 1-13
    • Arnau, J.1    Lauritzen, C.2    Petersen, G.E.3    Pedersen, J.4
  • 5
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • DOI 10.1074/jbc.272.50.31293
    • D. Lu, X. Yuan, X. Zheng, and J.E. Sadler Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain J. Biol. Chem. 272 1997 31293 31300 (Pubitemid 28013261)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.50 , pp. 31293-31300
    • Lu, D.1    Yuan, X.2    Zheng, X.3    Sadler, J.E.4
  • 8
    • 33646726556 scopus 로고    scopus 로고
    • Protease specificity determination by using cellular libraries of peptide substrates (CLiPS)
    • K.T. Boulware, and P.S. Daugherty Protease specificity determination by using cellular libraries of peptide substrates (CLiPS) Proc. Natl. Acad. Sci. USA 103 2006 7583 7588
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 7583-7588
    • Boulware, K.T.1    Daugherty, P.S.2
  • 9
    • 33847742147 scopus 로고    scopus 로고
    • The ways of realization of high specificity and efficiency of enteropeptidase
    • DOI 10.2174/092986607780090793
    • A.G. Mikhailova, V.V. Likhareva, N. Teich, and L.D. Rumsh The ways of realization of high specificity and efficiency of enteropeptidase Prot. Pep. Lett. 14 2007 227 232 (Pubitemid 46376852)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.3 , pp. 227-232
    • Mikhailova, A.G.1    Likhareva, V.V.2    Teich, N.3    Rumsh, L.D.4
  • 11
    • 23844507473 scopus 로고    scopus 로고
    • The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition
    • DOI 10.1074/jbc.M505661200
    • Z. Nemoda, and M. Sahin-Tóth The tetra-aspartate motif in the activation peptide of human cationic trypsinogen is essential for autoactivation control but not for enteropeptidase recognition J. Biol. Chem. 19 2005 29645 29652 (Pubitemid 41177040)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.33 , pp. 29645-29652
    • Nemoda, Z.1    Sahin-Toth, M.2
  • 14
    • 0141762591 scopus 로고    scopus 로고
    • Expression, purification, and characterization of human enteropeptidase catalytic subunit in Escherichia coli
    • DOI 10.1016/S1046-5928(03)00159-1
    • M.E. Gasparian, V.G. Ostapchenko, A.A. Schulga, D.A. Dolgikh, and M.P. Kirpichnikov Expression purification and characterization of human enteropeptidase catalytic subunit in Escherichia coli Protein Expr. Purif. 31 2003 133 139 (Pubitemid 37207651)
    • (2003) Protein Expression and Purification , vol.31 , Issue.1 , pp. 133-139
    • Gasparian, M.E.1    Ostapchenko, V.G.2    Schulga, A.A.3    Dolgikh, D.A.4    Kirpichnikov, M.P.5
  • 15
    • 34548125801 scopus 로고    scopus 로고
    • Overexpression and refolding of thioredoxin/TRAIL fusion from inclusion bodies and further purification of TRAIL after cleavage by enteropeptidase
    • DOI 10.1007/s10529-007-9446-y
    • M.E. Gasparian, V.G. Ostapchenko, A.V. Yagolovich, I.N. Tsygannik, B.V. Chernyak, D.A. Dolgikh, and M.P. Kirpichnikov Overexpression and refolding of thioredoxin/TRAIL fusion from inclusion bodies and further purification of TRAIL after cleavage by enteropeptidase Biotech. Lett. 29 2007 1567 1573 (Pubitemid 47301377)
    • (2007) Biotechnology Letters , vol.29 , Issue.10 , pp. 1567-1573
    • Gasparian, M.E.1    Ostapchenko, V.G.2    Yagolovich, A.V.3    Tsygannik, I.N.4    Chernyak, B.V.5    Dolgikh, D.A.6    Kirpichnikov, M.P.7
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • DOI 10.1016/j.tibtech.2005.03.012, PII S0167779905000843
    • D.S. Waugh Making the most of affinity tags Trends Biotechnol. 23 2005 316 320 (Pubitemid 40726273)
    • (2005) Trends in Biotechnology , vol.23 , Issue.6 , pp. 316-320
    • Waugh, D.S.1
  • 19
    • 79952200480 scopus 로고    scopus 로고
    • Tagging recombinant proteins to enhance solubility and aid purification
    • D. Walls, and S.T. Loughran Tagging recombinant proteins to enhance solubility and aid purification Methods Mol. Biol. 681 2011 151 175
    • (2011) Methods Mol. Biol. , vol.681 , pp. 151-175
    • Walls, D.1    Loughran, S.T.2
  • 20
    • 18144365489 scopus 로고    scopus 로고
    • Preparation of recombinant thioredoxin fused N-terminal proCNP: Analysis of enterokinase cleavage products reveals new enterokinase cleavage sites
    • DOI 10.1016/j.pep.2005.03.006
    • O.W. Liew, J.P. Ching Chong, T.G. Yandle, and S.O. Brennan Preparation of recombinant thioredoxin fused N-terminal proCNP: analysis of enterokinase cleavage products reveals new enterokinase cleavage sites Protein Expr. Purif. 41 2005 332 340 (Pubitemid 40607779)
    • (2005) Protein Expression and Purification , vol.41 , Issue.2 , pp. 332-340
    • Oi, W.L.1    Chong, J.P.C.2    Yandle, T.G.3    Brennan, S.O.4
  • 21
    • 42749093598 scopus 로고    scopus 로고
    • Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag
    • S.H. Shahravan, X. Qu, I.S. Chan, and J.A. Shin Enhancing the specificity of the enterokinase cleavage reaction to promote efficient cleavage of a fusion tag Protein Expr. Purif. 59 2008 314 319
    • (2008) Protein Expr. Purif. , vol.59 , pp. 314-319
    • Shahravan, S.H.1    Qu, X.2    Chan, I.S.3    Shin, J.A.4
  • 22
    • 34548431285 scopus 로고    scopus 로고
    • Purification and characterization of a recombinant rat prohaptoglobin expressed in baculovirus-infected Sf9 insect cells
    • DOI 10.1016/j.pep.2007.06.004, PII S1046592807001593
    • A. Hillar, G. Otulakowski, and H. Brodovich Purification and characterization of a recombinant rat prohaptoglobin expressed in baculovirus-infected Sf9 insect cells Protein Expr. Purif. 55 2007 246 256 (Pubitemid 47369663)
    • (2007) Protein Expression and Purification , vol.55 , Issue.2 , pp. 246-256
    • Hillar, A.1    Otulakowski, G.2    O'Brodovich, H.3
  • 23
    • 0033541686 scopus 로고    scopus 로고
    • 4Lys on enterokinase cleavage of a fusion protein
    • DOI 10.1006/abio.1998.3084
    • T. Hosfield, and Q. Lu Influence of the amino acid residue downstream of (Asp)4Lys on enterokinase cleavage of a fusion protein Anal. Biochem. 269 1999 10 16 (Pubitemid 29174256)
    • (1999) Analytical Biochemistry , vol.269 , Issue.1 , pp. 10-16
    • Hosfield, T.1    Lu, Q.2
  • 24
    • 0021827776 scopus 로고
    • Redesigning trypsin: Alteration of substrate specificity
    • C.S. Craik, C. Largman, T. Fletcher, S. Roczniak, P.J. Barr, R. Fletterick, and W.J. Rutter Redesigning trypsin: alteration of substrate specificity Science 228 1985 291 297 (Pubitemid 15076825)
    • (1985) Science , vol.228 , Issue.4697 , pp. 291-297
    • Craik, C.S.1    Largman, C.2    Fletcher, T.3
  • 25
    • 79952198939 scopus 로고    scopus 로고
    • Tag removal by site-specific cleavage of recombinant fusion proteins
    • A. Charlton, and M. Zachariou Tag removal by site-specific cleavage of recombinant fusion proteins Methods Mol. Biol. 681 2011 349 367
    • (2011) Methods Mol. Biol. , vol.681 , pp. 349-367
    • Charlton, A.1    Zachariou, M.2
  • 26
    • 0344631102 scopus 로고    scopus 로고
    • Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide
    • DOI 10.1006/jmbi.1999.3089
    • D. Lu, K. Fütterer, S. Korolev, X. Zheng, K. Tan, G. Waksman, and J.E. Sadler Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide J. Mol. Biol. 292 1999 361 373 (Pubitemid 29435772)
    • (1999) Journal of Molecular Biology , vol.292 , Issue.2 , pp. 361-373
    • Lu, D.1    Futterer, K.2    Korolev, S.3    Zheng, X.4    Tan, K.5    Waksman, G.6    Sadler, J.E.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.