메뉴 건너뛰기




Volumn 37, Issue 3, 2007, Pages 205-217

Functional expression and purification of bovine enterokinase light chain in recombinant Escherichia coli

Author keywords

Bovine enterokinase light chain; Enterokinase; Enzyme activity; Escherichia coli; Fusion expression; Purification

Indexed keywords

ENTEROPEPTIDASE; HIS HIS HIS HIS HIS HIS; HIS-HIS-HIS-HIS-HIS-HIS; HISTIDINE; HYBRID PROTEIN; ISOPROPYL THIOGALACTOSIDE; OLIGOPEPTIDE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34249089817     PISSN: 10826068     EISSN: 15322297     Source Type: Journal    
DOI: 10.1080/10826060701386695     Document Type: Article
Times cited : (17)

References (22)
  • 1
    • 0015239936 scopus 로고
    • Purification and specificity of porcine enterokinase
    • Maroux, S.; Baratti, J.; Desnuelle, P. Purification and specificity of porcine enterokinase. J. Biol. Chem. 1971, 246, 5031-5039.
    • (1971) J. Biol. Chem , vol.246 , pp. 5031-5039
    • Maroux, S.1    Baratti, J.2    Desnuelle, P.3
  • 2
    • 0015785910 scopus 로고
    • On porcine enterokinase. Further purification and some molecular properties
    • Baratti, J.; Maroux, S.; Louvard, D.; Desnuelle, P. On porcine enterokinase. Further purification and some molecular properties. Biochim. Biophys. Acta 1973, 315, 147-161.
    • (1973) Biochim. Biophys. Acta , vol.315 , pp. 147-161
    • Baratti, J.1    Maroux, S.2    Louvard, D.3    Desnuelle, P.4
  • 3
    • 0017727892 scopus 로고
    • Bovine enterokinase. Purification, specificity, and some molecular properties
    • Anderson, L.E.; Walsh, K.A.; Neurath, H. Bovine enterokinase. Purification, specificity, and some molecular properties. Biochemistry 1977, 16, 3354-3360.
    • (1977) Biochemistry , vol.16 , pp. 3354-3360
    • Anderson, L.E.1    Walsh, K.A.2    Neurath, H.3
  • 4
    • 0018786255 scopus 로고
    • The preparation and properties of bovine enterokinase
    • Liepnieks, J.J.; Lighe, A. The preparation and properties of bovine enterokinase. J. Biol. Chem. 1979, 254, 1677-1683.
    • (1979) J. Biol. Chem , vol.254 , pp. 1677-1683
    • Liepnieks, J.J.1    Lighe, A.2
  • 5
    • 0021099291 scopus 로고
    • The purification and characterization of bovine enterokinase from membrane fragment in the duodenal mucosal fluid
    • Fonseca, P.; Light, A. The purification and characterization of bovine enterokinase from membrane fragment in the duodenal mucosal fluid. J. Biol. Chem. 1983, 258, 3069-3074.
    • (1983) J. Biol. Chem , vol.258 , pp. 3069-3074
    • Fonseca, P.1    Light, A.2
  • 6
    • 0019469219 scopus 로고
    • Further studies on the subunit structure and oligosaccharide moiety of human enterokinase
    • Magee, A.I.; Grant, D.A.; Taylor, J.H. Further studies on the subunit structure and oligosaccharide moiety of human enterokinase. Clin. Chim. Acta 1981, 115, 241-254.
    • (1981) Clin. Chim. Acta , vol.115 , pp. 241-254
    • Magee, A.I.1    Grant, D.A.2    Taylor, J.H.3
  • 7
    • 0344631102 scopus 로고    scopus 로고
    • Crystal structure of enteropeptidase light chain complexed with an anolog of the trypsinogen activation peptide
    • Lu, D.; Futterer, K.; Korolev, S.; Zheng, X.; Tan, K.; Waksman, G.; Sadler, J.E. Crystal structure of enteropeptidase light chain complexed with an anolog of the trypsinogen activation peptide. J. Mol. Biol. 1999, 292, 361-373.
    • (1999) J. Mol. Biol , vol.292 , 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
  • 9
    • 0029115204 scopus 로고
    • Production of a recombinant bovine enterokinase catalytic submit in Escherichia coli using the novel secretory fusion partner DsbA
    • Collins, L.A.; McColgan, J.M.; Grant, K.L.; DiBlasio, E.A.; McCoy, J.M.; LaVallie, E.R. Production of a recombinant bovine enterokinase catalytic submit in Escherichia coli using the novel secretory fusion partner DsbA. Bio/Technology 1995, 13, 982-987.
    • (1995) Bio/Technology , vol.13 , pp. 982-987
    • Collins, L.A.1    McColgan, J.M.2    Grant, K.L.3    DiBlasio, E.A.4    McCoy, J.M.5    LaVallie, E.R.6
  • 10
    • 0036425999 scopus 로고    scopus 로고
    • Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli
    • Yuan, L.D.; Hua, Z.C. Expression, purification, and characterization of a biologically active bovine enterokinase catalytic subunit in Escherichia coli. Protein Exper. Purif. 2002, 25, 300-304.
    • (2002) Protein Exper. Purif , vol.25 , pp. 300-304
    • Yuan, L.D.1    Hua, Z.C.2
  • 12
    • 0842302982 scopus 로고    scopus 로고
    • High-level secretory production of recombinant bovine enterokinase light chain by Pichia pastoris
    • Peng, L.; Zhong, X.; Ou, J.; Zheng, S.; Liao, J.; Wang, L.; Xu, A. High-level secretory production of recombinant bovine enterokinase light chain by Pichia pastoris. J. Biotechnol. 2004, 108, 185-192.
    • (2004) J. Biotechnol , vol.108 , pp. 185-192
    • Peng, L.1    Zhong, X.2    Ou, J.3    Zheng, S.4    Liao, J.5    Wang, L.6    Xu, A.7
  • 13
    • 0344339091 scopus 로고    scopus 로고
    • Expression of catalytic subunit of bovine enterokinase in the filamentous fungus Aspergillus niger
    • Svetina, M.; Krasevec, N.; Gaberc, V.; Komel, R. Expression of catalytic subunit of bovine enterokinase in the filamentous fungus Aspergillus niger. J. Biotechnol. 2000, 76, 245-251.
    • (2000) J. Biotechnol , vol.76 , pp. 245-251
    • Svetina, M.1    Krasevec, N.2    Gaberc, V.3    Komel, R.4
  • 14
    • 0035924096 scopus 로고    scopus 로고
    • Recombinant enterokinase light chain with affinity tag, expression from Saccharomyces cerevisiae and its utilities in fusion protein technology
    • Choi, S.I.; Song, H.W.; Moon, J.W.; Seong, B.L. Recombinant enterokinase light chain with affinity tag, expression from Saccharomyces cerevisiae and its utilities in fusion protein technology. Biotechnol. Bioeng. 2001, 75, 718-724.
    • (2001) Biotechnol. Bioeng , vol.75 , pp. 718-724
    • Choi, S.I.1    Song, H.W.2    Moon, J.W.3    Seong, B.L.4
  • 15
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane, J.F. Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 1995, 6, 494-500.
    • (1995) Curr. Opin. Biotechnol , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 16
    • 3142662719 scopus 로고    scopus 로고
    • Preferential Codons Enhancing the Expression Level of Human Beta-Defensin-2
    • Peng, L.; Xu, Z.N.; Fang, X.M.; Wang, F.; Yang, S.; Cen, P.L. Preferential Codons Enhancing the Expression Level of Human Beta-Defensin-2. Protein Peptide Lett. 2004, 11, 339-344.
    • (2004) Protein Peptide Lett , vol.11 , pp. 339-344
    • Peng, L.1    Xu, Z.N.2    Fang, X.M.3    Wang, F.4    Yang, S.5    Cen, P.L.6
  • 17
    • 33747735624 scopus 로고    scopus 로고
    • High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression
    • Xu, Z.N.; Zhong, Z.X.; Huang, L.; Peng, L.; Wang, F.; Cen, P.L. High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression. Appl. Microbiol. Biotechnol. 2006, 72, 471-479.
    • (2006) Appl. Microbiol. Biotechnol , vol.72 , pp. 471-479
    • Xu, Z.N.1    Zhong, Z.X.2    Huang, L.3    Peng, L.4    Wang, F.5    Cen, P.L.6
  • 18
    • 0030151989 scopus 로고    scopus 로고
    • Specific replacement of consecutive AGG codons results in high-level expression of human cardiac troponin T in Escherichia coli
    • Hu, X.Y.; Shi, Q.W.; Yang, T.; Jackowski, G. Specific replacement of consecutive AGG codons results in high-level expression of human cardiac troponin T in Escherichia coli. Protein Express. Purif. 1996, 7, 289-293.
    • (1996) Protein Express. Purif , vol.7 , pp. 289-293
    • Hu, X.Y.1    Shi, Q.W.2    Yang, T.3    Jackowski, G.4
  • 20
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • Lu, D.; Yuan, X.; Zheng, X.; Sadler, J.E. Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain. J. Biol. Chem. 1997, 272, 31293-31300.
    • (1997) J. Biol. Chem , vol.272 , pp. 31293-31300
    • Lu, D.1    Yuan, X.2    Zheng, X.3    Sadler, J.E.4
  • 21
    • 0036544572 scopus 로고    scopus 로고
    • Engineered recombinant enteropeptidase catalytic subunit, effect of N-terminal modification
    • Song, H.; Choi, S.; Seong, B.L. Engineered recombinant enteropeptidase catalytic subunit, effect of N-terminal modification. Arch. Biochem. Biophys. 2002, 400, 1-6.
    • (2002) Arch. Biochem. Biophys , vol.400 , pp. 1-6
    • Song, H.1    Choi, S.2    Seong, B.L.3
  • 22
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulfide bond formation in vivo
    • Martin, J.L.; Bardwell, J.C.A.; Kuriyan, J. Crystal structure of the DsbA protein required for disulfide bond formation in vivo. Nature 1993, 365, 64-468.
    • (1993) Nature , vol.365 , pp. 64-468
    • Martin, J.L.1    Bardwell, J.C.A.2    Kuriyan, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.