메뉴 건너뛰기




Volumn 34, Issue 2, 2007, Pages 114-121

Production of MBP-HepA fusion protein in recombinant Escherichia coli by optimization of culture medium

Author keywords

Fusion protein; HepA; MBP; Orthogonal experimental design; Recombinant Escherichia coli; Vector modification

Indexed keywords

FUSION PROTEIN; ORTHOGONAL EXPERIMENTAL DESIGN; RECOMBINANT ESCHERICHIA COLI; VECTOR MODIFICATION;

EID: 33947305443     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2006.11.020     Document Type: Article
Times cited : (46)

References (27)
  • 2
    • 0032516052 scopus 로고    scopus 로고
    • Direct evidence for a predominantly exolytic processive mechanism for depolymerization of heparin-like glycosaminoglycans by heparinase I
    • Ernst S., Rhomberg A.J., Biemann K., and Sasisekharan R. Direct evidence for a predominantly exolytic processive mechanism for depolymerization of heparin-like glycosaminoglycans by heparinase I. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 4182-4187
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 4182-4187
    • Ernst, S.1    Rhomberg, A.J.2    Biemann, K.3    Sasisekharan, R.4
  • 4
    • 0021920714 scopus 로고
    • Purification and characterization of heparinase from Flavobacterium heparinum
    • Yang V.C., Linhardt R.J., Bernstein H., Cooney C.L., and Langer R. Purification and characterization of heparinase from Flavobacterium heparinum. J. Biol. Chem. 260 (1985) 1849-1857
    • (1985) J. Biol. Chem. , vol.260 , pp. 1849-1857
    • Yang, V.C.1    Linhardt, R.J.2    Bernstein, H.3    Cooney, C.L.4    Langer, R.5
  • 6
    • 0029876949 scopus 로고    scopus 로고
    • Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum
    • Ernst S., Venkataraman G., Winkler S., Godavarti R., Langer R., Cooney C.L., and Sasisekharan R. Expression in Escherichia coli, purification and characterization of heparinase I from Flavobacterium heparinum. Biochem. J. 315 (1996) 589-597
    • (1996) Biochem. J. , vol.315 , pp. 589-597
    • Ernst, S.1    Venkataraman, G.2    Winkler, S.3    Godavarti, R.4    Langer, R.5    Cooney, C.L.6    Sasisekharan, R.7
  • 8
    • 13244268462 scopus 로고    scopus 로고
    • Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein
    • Chen Y., Xing X.H., and Lou K. Construction of recombinant Escherichia coli for over-production of soluble heparinase I by fusion to maltose-binding protein. Biochem. Eng. J. 23 (2005) 155-159
    • (2005) Biochem. Eng. J. , vol.23 , pp. 155-159
    • Chen, Y.1    Xing, X.H.2    Lou, K.3
  • 9
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust R.B., and Waugh D.S. 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
  • 10
    • 33750633211 scopus 로고    scopus 로고
    • Production of heparin oligosaccharides by fusion protein of MBP-heparinase I and the enzymatic thermostability
    • Kuang Y., Xing X.-H., Chen Y., Ye F.C., Chen Y., Yang Y.Y., Liu Z., and Bi R.C. Production of heparin oligosaccharides by fusion protein of MBP-heparinase I and the enzymatic thermostability. J. Mol. Catal. B: Enzym. 43 (2006) 90-95
    • (2006) J. Mol. Catal. B: Enzym. , vol.43 , pp. 90-95
    • Kuang, Y.1    Xing, X.-H.2    Chen, Y.3    Ye, F.C.4    Chen, Y.5    Yang, Y.Y.6    Liu, Z.7    Bi, R.C.8
  • 11
    • 0036139997 scopus 로고    scopus 로고
    • Amperometric TNT biosensor based on the oriented immobilization of a nitroreductase maltose binding protein fusion
    • Naal Z., Park J.H., Bernhard S., Shapleigh J.P., Batt C.A., and Abruna H.D. Amperometric TNT biosensor based on the oriented immobilization of a nitroreductase maltose binding protein fusion. Anal. Chem. 74 (2002) 140-148
    • (2002) Anal. Chem. , vol.74 , pp. 140-148
    • Naal, Z.1    Park, J.H.2    Bernhard, S.3    Shapleigh, J.P.4    Batt, C.A.5    Abruna, H.D.6
  • 12
    • 0033548130 scopus 로고    scopus 로고
    • The calcium-binding sites of heparinase I from Flavobacterium heparinum are essential for enzymatic activity
    • Liu D., Shriver Z., Godavarti R., Venkataraman G., and Sasisekharan R. The calcium-binding sites of heparinase I from Flavobacterium heparinum are essential for enzymatic activity. J. Biol. Chem. 274 (1999) 4089-4095
    • (1999) J. Biol. Chem. , vol.274 , pp. 4089-4095
    • Liu, D.1    Shriver, Z.2    Godavarti, R.3    Venkataraman, G.4    Sasisekharan, R.5
  • 13
    • 0025862114 scopus 로고
    • Medium optimization by an orthogonal array design for the growth of Methanosarcina barkeri
    • Silveira R.G., Kakizono T., Takemoto S., Nishio N., and Nagai S. Medium optimization by an orthogonal array design for the growth of Methanosarcina barkeri. J. Ferm. Bioeng. 72 (1991) 20-25
    • (1991) J. Ferm. Bioeng. , vol.72 , pp. 20-25
    • Silveira, R.G.1    Kakizono, T.2    Takemoto, S.3    Nishio, N.4    Nagai, S.5
  • 14
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 31 (1959) 426-428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 16
    • 0029777326 scopus 로고    scopus 로고
    • Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum
    • Su H., Blain F., Musil R.A., Zimmermann J.J., Gu K., and Bennett D.C. Isolation and expression in Escherichia coli of hepB and hepC, genes coding for the glycosaminoglycan-degrading enzymes heparinase II and heparinase III, respectively, from Flavobacterium heparinum. Appl. Environ. Microbiol. 62 (1996) 2723-2734
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2723-2734
    • Su, H.1    Blain, F.2    Musil, R.A.3    Zimmermann, J.J.4    Gu, K.5    Bennett, D.C.6
  • 17
    • 25844443463 scopus 로고    scopus 로고
    • Expression of human peripheral cannabinoid receptor for structural studies
    • Yeliseev A.A., Wong K.K., Soubias O., and Gawrisch K. Expression of human peripheral cannabinoid receptor for structural studies. Protein Sci. 14 (2005) 2638-2653
    • (2005) Protein Sci. , vol.14 , pp. 2638-2653
    • Yeliseev, A.A.1    Wong, K.K.2    Soubias, O.3    Gawrisch, K.4
  • 18
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli
    • Weiss H.M., and Grisshammer R. Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur. J. Biochem. 269 (2002) 82-92
    • (2002) Eur. J. Biochem. , vol.269 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 19
    • 1942468187 scopus 로고    scopus 로고
    • Automated large-scale purification of a G protein-coupled receptor for neurotensin
    • White J.F., Trinh L.B., Shiloach J., and Grisshammer R. Automated large-scale purification of a G protein-coupled receptor for neurotensin. FEBS Lett. 564 (2004) 289-293
    • (2004) FEBS Lett. , vol.564 , pp. 289-293
    • White, J.F.1    Trinh, L.B.2    Shiloach, J.3    Grisshammer, R.4
  • 20
    • 0033548178 scopus 로고    scopus 로고
    • Biochemical investigations and mapping the calcium-binding sites of heparinase I from Flavobacterium heparinum
    • Shriver Z., liu D., Hu Y., and Sasisekharan R. Biochemical investigations and mapping the calcium-binding sites of heparinase I from Flavobacterium heparinum. J. Biol. Chem. 274 (1999) 4082-4088
    • (1999) J. Biol. Chem. , vol.274 , pp. 4082-4088
    • Shriver, Z.1    liu, D.2    Hu, Y.3    Sasisekharan, R.4
  • 21
    • 0031887212 scopus 로고    scopus 로고
    • Characterization of heparinase from an oral bacterium Prevotella heparinolytica
    • Watanabe M., Tsuda H., Yamada S., Shibata Y., Nakamura T., and Sugahara K. Characterization of heparinase from an oral bacterium Prevotella heparinolytica. J. Biochem. 123 (1998) 283-288
    • (1998) J. Biochem. , vol.123 , pp. 283-288
    • Watanabe, M.1    Tsuda, H.2    Yamada, S.3    Shibata, Y.4    Nakamura, T.5    Sugahara, K.6
  • 22
    • 0033844117 scopus 로고    scopus 로고
    • Purification and characterization of a novel heparinase from Bacteroides stercoris HJ-15
    • Kim B.T., Kim W.S., Kim Y.S., Linhardt R.J., and Kim D.H. Purification and characterization of a novel heparinase from Bacteroides stercoris HJ-15. J. Biochem. 128 (2000) 323-328
    • (2000) J. Biochem. , vol.128 , pp. 323-328
    • Kim, B.T.1    Kim, W.S.2    Kim, Y.S.3    Linhardt, R.J.4    Kim, D.H.5
  • 23
    • 0343196718 scopus 로고    scopus 로고
    • Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21(DE3)[pET-3aT2M2]
    • Shin C.S., Hong M.S., Bae C.S., and Lee J. Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21(DE3)[pET-3aT2M2]. Biotechnol. Prog. 13 (1997) 249-257
    • (1997) Biotechnol. Prog. , vol.13 , pp. 249-257
    • Shin, C.S.1    Hong, M.S.2    Bae, C.S.3    Lee, J.4
  • 24
    • 0030670056 scopus 로고    scopus 로고
    • Process optimization for large-scale production of TGF-a-PE40 in recombinant Escherichia coli: effect of medium composition and induction timing on protein expression
    • Lee C., Sun W.J., Burgess B.W., Junker B.H., Reddy J., Buckland B.C., and Greasham R.L. Process optimization for large-scale production of TGF-a-PE40 in recombinant Escherichia coli: effect of medium composition and induction timing on protein expression. J. Ind. Microbiol. Biotechnol. 18 (1997) 260-266
    • (1997) J. Ind. Microbiol. Biotechnol. , vol.18 , pp. 260-266
    • Lee, C.1    Sun, W.J.2    Burgess, B.W.3    Junker, B.H.4    Reddy, J.5    Buckland, B.C.6    Greasham, R.L.7
  • 25
    • 2942557320 scopus 로고    scopus 로고
    • M.I. Viitanen, A. Vasala, P. Neubauer, T. Alatossava, Cheese whey-induced high-cell-density production of recombinant proteins in Escherichia coli, Microbial Cell Factories 2:2, 2003.
  • 26
    • 19544381068 scopus 로고    scopus 로고
    • Growing E. coli to high cell density-a historical perspective on method development
    • Shiloach J., and Fass R. Growing E. coli to high cell density-a historical perspective on method development. Biotechnol. Adv. 23 (2005) 345-357
    • (2005) Biotechnol. Adv. , vol.23 , pp. 345-357
    • Shiloach, J.1    Fass, R.2
  • 27
    • 0026460982 scopus 로고
    • Purification and characterization of heparin lyases from Flavobacterium heparinum
    • Lohse D.L., and Linhardt R.J. Purification and characterization of heparin lyases from Flavobacterium heparinum. J. Biol. Chem. 276 (1992) 24347-24355
    • (1992) J. Biol. Chem. , vol.276 , pp. 24347-24355
    • Lohse, D.L.1    Linhardt, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.