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Volumn 25, Issue 2, 2002, Pages 300-304

Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALS; CATALYSIS; CATALYTIC DOMAIN; CATTLE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENTEROPEPTIDASE; ESCHERICHIA COLI; KINETICS; PLASMIDS; RECOMBINANT PROTEINS;

EID: 0036425999     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1046-5928(02)00012-8     Document Type: Article
Times cited : (36)

References (16)
  • 1
    • 0029980434 scopus 로고    scopus 로고
    • Renaturation of recombinant human pro-urokinase expressed in Escherichia coli
    • Z.C. Hua, C. Dong, D.X. Zhu, Renaturation of recombinant human pro-urokinase expressed in Escherichia coli, Biochem. Biophys. Res. Commun. 220 (1996) 131-136.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 131-136
    • Hua, Z.C.1    Dong, C.2    Zhu, D.X.3
  • 2
    • 0030941068 scopus 로고    scopus 로고
    • Renaturation and purification of recombinant tissue-type plasminogen activator expressed in Escherichia coli
    • Z.C. Hua, Renaturation and purification of recombinant tissue-type plasminogen activator expressed in Escherichia coli, Biochem. Mol. Biol. Int. 41 (1997) 815-820.
    • (1997) Biochem. Mol. Biol. Int. , vol.41 , pp. 815-820
    • Hua, Z.C.1
  • 3
    • 0029814723 scopus 로고    scopus 로고
    • Enhancement of in vitro renaturation of recombinant human pro-urokinase by ampicillin
    • Z.C. Hua, C. Dong, D.X. Zhu, Enhancement of in vitro renaturation of recombinant human pro-urokinase by ampicillin, Biochem. Mol. Biol. Int. 39 (1996) 1093-1097.
    • (1996) Biochem. Mol. Biol. Int. , vol.39 , pp. 1093-1097
    • Hua, Z.C.1    Dong, C.2    Zhu, D.X.3
  • 4
    • 0022053837 scopus 로고
    • Immobilization and purification of enzyme with Staphylococcal protein A gene fusion vectors
    • B. Nilsson, L. Abrahmsen, M. Uhlen, Immobilization and purification of enzyme with Staphylococcal protein A gene fusion vectors, EMBO J. (1985) 4,1075-1080.
    • (1985) EMBO J. , pp. 4
    • Nilsson, B.1    Abrahmsen, L.2    Uhlen, M.3
  • 5
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase
    • D.B. Smith, K.S. Johnson, Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione-S-transferase, Gene 67 (1988) 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 6
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • C.V. Maina, P.D. Riggs, A.G. Grandea, B.E. Slatko, L.S. Moran, J.A. Tagliamonte, L.A. McReynolds, C. di Guan, An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein, Gene 74 (1988) 365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5    Tagliamonte, J.A.6    McReynolds, L.A.7    Di Guan, C.8
  • 7
    • 14744292185 scopus 로고
    • A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
    • E.R. LaVallie, E.A. DiBlasio, S. Kovacic, K.L. Grant, P.F. Schendel, J.M. McCoy, A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm, Bio-Technol. 11 (1993) 187-193.
    • (1993) Bio-Technol. , vol.11 , pp. 187-193
    • LaVallie, E.R.1    DiBlasio, E.A.2    Kovacic, S.3    Grant, K.L.4    Schendel, P.F.5    McCoy, J.M.6
  • 9
    • 0029115204 scopus 로고
    • Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA
    • L.A. Collins-Racie, J.M. McColgan, K.L. Grant, E.A. DiBlasio-Smith, J.M. McCoy, E.R. LaVallie, Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA, Bio-Technol. 13 (1995) 982-987.
    • (1995) Bio-Technol. , vol.13 , pp. 982-987
    • Collins-Racie, L.A.1    McColgan, J.M.2    Grant, K.L.3    DiBlasio-Smith, E.A.4    McCoy, J.M.5    LaVallie, E.R.6
  • 11
    • 0034049054 scopus 로고    scopus 로고
    • Expression of human cardiac-specific homeobox protein (hCsx) in Escherichia coli
    • J.H. Zhao, Z. Xu, Z.C. Hua, Expression of human cardiac-specific homeobox protein (hCsx) in Escherichia coli, Protein Expres. Purif. 18 (2000) 316-319.2.
    • (2000) Protein Expres. Purif. , vol.18 , pp. 316-3192
    • Zhao, J.H.1    Xu, Z.2    Hua, Z.C.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0018344418 scopus 로고
    • Hydrolysis of artificial substrates by enterokinase and trypsin and the development of a sensitive specific assay for enterokinase in serum
    • D.A.W. Grant, J. Hermon-Taylor, Hydrolysis of artificial substrates by enterokinase and trypsin and the development of a sensitive specific assay for enterokinase in serum, Biochim. Biophys. Acta 567 (1979) 207-215.
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 207-215
    • Grant, D.A.W.1    Hermon-Taylor, J.2
  • 14
    • 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
  • 15
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • D. Lu, X. Yuan, X. Zheng, J. Evan Sadler, Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain, J. Bio. Chem. 272 (1997) 31293-31300.
    • (1997) J. Bio. Chem. , vol.272 , pp. 31293-31300
    • Lu, D.1    Yuan, X.2    Zheng, X.3    Evan Sadler, J.4
  • 16
    • 0033541686 scopus 로고    scopus 로고
    • 4Lys on enterokinase cleavage of a fusion protein
    • 4Lys on enterokinase cleavage of a fusion protein, Anal. Biochem. 269 (1999) 10-16.
    • (1999) Anal. Biochem. , vol.269 , pp. 10-16
    • Hosfield, T.1    Lu, Q.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.