메뉴 건너뛰기




Volumn 38, Issue 1, 2004, Pages 29-36

Extracellular expression and single step purification of recombinant Escherichia coli l-asparaginase II

Author keywords

Acute lymphoblastic leukemia; Escherichia coli; Extracellular expression; Recombinant asparaginase

Indexed keywords

ASPARAGINASE; RECOMBINANT PROTEIN;

EID: 5344224839     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.07.009     Document Type: Article
Times cited : (107)

References (35)
  • 1
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • S.C. Makrides Strategies for achieving high-level expression of genes in Escherichia coli Microbiol. Rev. 60 1996 512 538
    • (1996) Microbiol. Rev. , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 2
    • 0033772459 scopus 로고    scopus 로고
    • Expressing genes in different Escherichia coli compartments
    • P. Cornelis Expressing genes in different Escherichia coli compartments Curr. Opin. Biotechnol. 11 2000 450 454
    • (2000) Curr. Opin. Biotechnol. , vol.11 , pp. 450-454
    • Cornelis, P.1
  • 3
    • 0036204976 scopus 로고    scopus 로고
    • Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli
    • P. Jonasson, S. Liljeqvist, P.A. Nygren, and S. Stahl Genetic design for facilitated production and recovery of recombinant proteins in Escherichia coli Biotechnol. Appl. Biochem. 35 2002 91 105
    • (2002) Biotechnol. Appl. Biochem. , vol.35 , pp. 91-105
    • Jonasson, P.1    Liljeqvist, S.2    Nygren, P.A.3    Stahl, S.4
  • 5
    • 0031988031 scopus 로고    scopus 로고
    • Secretion of proteins and assembly of bacterial surface organelles: Shared pathways of extracellular protein targeting
    • S. Lory Secretion of proteins and assembly of bacterial surface organelles: shared pathways of extracellular protein targeting Curr. Opin. Microbiol. 1 1998 27 35
    • (1998) Curr. Opin. Microbiol. , vol.1 , pp. 27-35
    • Lory, S.1
  • 6
    • 0031024552 scopus 로고    scopus 로고
    • Extracellular production of a hybrid beta-glucanase from Bacillus by Escherichia coli under different cultivation conditions in shaking cultures and bioreactors
    • G. Miksch, R. Neitzel, E. Fiedler, K. Friehs, and E. Flaschel Extracellular production of a hybrid beta-glucanase from Bacillus by Escherichia coli under different cultivation conditions in shaking cultures and bioreactors Appl. Microbiol. Biotechnol. 47 1997 120 126
    • (1997) Appl. Microbiol. Biotechnol. , vol.47 , pp. 120-126
    • Miksch, G.1    Neitzel, R.2    Fiedler, E.3    Friehs, K.4    Flaschel, E.5
  • 7
    • 0344950388 scopus 로고    scopus 로고
    • Secretory expression in Escherichia coli and single-step purification of a heat-stable alkaline protease
    • Z. Fu, S.B. Hamid, C.N. Razak, M. Basri, A.B. Salleh, and R.N. Rahman Secretory expression in Escherichia coli and single-step purification of a heat-stable alkaline protease Protein Expr. Purif. 28 2003 63 68
    • (2003) Protein Expr. Purif. , vol.28 , pp. 63-68
    • Fu, Z.1    Hamid, S.B.2    Razak, C.N.3    Basri, M.4    Salleh, A.B.5    Rahman, R.N.6
  • 8
    • 0032190602 scopus 로고    scopus 로고
    • TolA III co-overexpression facilitates the recovery of periplasmic recombinant proteins into the growth medium of Escherichia coli
    • E.W. Wan, and F. Baneyx TolA III co-overexpression facilitates the recovery of periplasmic recombinant proteins into the growth medium of Escherichia coli Protein Expr. Purif. 14 1998 13 22
    • (1998) Protein Expr. Purif. , vol.14 , pp. 13-22
    • Wan, E.W.1    Baneyx, F.2
  • 9
    • 0026609772 scopus 로고
    • Protein release in recombinant Escherichia coli using bacteriocin release protein
    • P. Yu, and K.Y. San Protein release in recombinant Escherichia coli using bacteriocin release protein Biotechnol. Prog. 8 1992 25 29
    • (1992) Biotechnol. Prog. , vol.8 , pp. 25-29
    • Yu, P.1    San, K.Y.2
  • 10
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • G. Hannig, and S.C. Makrides Strategies for optimizing heterologous protein expression in Escherichia coli Trends Biotechnol. 16 1998 54 60
    • (1998) Trends Biotechnol. , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 11
    • 0032190666 scopus 로고    scopus 로고
    • Use of cell wall-less bacteria (L-forms) for efficient expression and secretion of heterologous gene products
    • J. Gumpert, and C. Hoischen Use of cell wall-less bacteria (L-forms) for efficient expression and secretion of heterologous gene products Curr. Opin. Biotechnol. 9 1998 506 509
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 506-509
    • Gumpert, J.1    Hoischen, C.2
  • 12
    • 0031973556 scopus 로고    scopus 로고
    • Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell-wall-less L-form strains of Proteus mirabilis and Escherichia coli: A comparison of the synthesis capacities of L-form strains with an E. coli producer strain
    • M.J. Kujau, C. Hoischen, D. Riesenberg, and J. Gumpert Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell-wall-less L-form strains of Proteus mirabilis and Escherichia coli: a comparison of the synthesis capacities of L-form strains with an E. coli producer strain Appl. Microbiol. Biotechnol. 49 1998 51 58
    • (1998) Appl. Microbiol. Biotechnol. , vol.49 , pp. 51-58
    • Kujau, M.J.1    Hoischen, C.2    Riesenberg, D.3    Gumpert, J.4
  • 13
    • 0024826985 scopus 로고
    • Heterologous protein export in Escherichia coli: Influence of bacterial signal peptides on the export of human interleukin 1 beta
    • P. Denefle, S. Kovarik, T. Ciora, N. Gosselet, J.C. Benichou, M. Latta, F. Guinet, A. Ryter, and J.F. Mayaux Heterologous protein export in Escherichia coli: influence of bacterial signal peptides on the export of human interleukin 1 beta Gene 85 1989 499 510
    • (1989) Gene , vol.85 , pp. 499-510
    • Denefle, P.1    Kovarik, S.2    Ciora, T.3    Gosselet, N.4    Benichou, J.C.5    Latta, M.6    Guinet, F.7    Ryter, A.8    Mayaux, J.F.9
  • 15
    • 0011864425 scopus 로고
    • Fusions of secreted proteins to alkaline phosphatase: An approach for studying protein secretion
    • C.S. Hoffman, and A. Wright Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion Proc. Natl. Acad. Sci. USA 82 1985 5107 5111
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 5107-5111
    • Hoffman, C.S.1    Wright, A.2
  • 16
    • 0037294121 scopus 로고    scopus 로고
    • Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli
    • A. Shokri, A.M. Sanden, and G. Larsson Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli Appl. Microbiol. Biotechnol. 60 2003 654 664
    • (2003) Appl. Microbiol. Biotechnol. , vol.60 , pp. 654-664
    • Shokri, A.1    Sanden, A.M.2    Larsson, G.3
  • 17
    • 0034135428 scopus 로고    scopus 로고
    • Secretory production of human leptin in Escherichia coli
    • J. Jeong, and S.Y. Lee Secretory production of human leptin in Escherichia coli Biotechnol. Bioeng. 67 2000 398 407
    • (2000) Biotechnol. Bioeng. , vol.67 , pp. 398-407
    • Jeong, J.1    Lee, S.Y.2
  • 18
    • 0030000710 scopus 로고    scopus 로고
    • Increased efficiency of alkaline phosphatase production levels in Escherichia coli using a degenerate pelB signal sequence
    • H. Le Calvez, J.M. Green, and D. Baty Increased efficiency of alkaline phosphatase production levels in Escherichia coli using a degenerate pelB signal sequence Gene 170 1996 51 55
    • (1996) Gene , vol.170 , pp. 51-55
    • Le Calvez, H.1    Green, J.M.2    Baty, D.3
  • 19
  • 20
    • 0028339881 scopus 로고
    • Thirty-three amino acids of the mature moiety of an unprocessed maltose-binding protein are sufficient for export in Escherichia coli
    • A. Barkocy-Gallagher, J.G. Cannon, and P.J. Bassford Jr. Thirty-three amino acids of the mature moiety of an unprocessed maltose-binding protein are sufficient for export in Escherichia coli J. Bacteriol. 176 1994 3397 3399
    • (1994) J. Bacteriol. , vol.176 , pp. 3397-3399
    • Barkocy-Gallagher, A.1    Cannon, J.G.2    Bassford Jr., P.J.3
  • 21
    • 0037393709 scopus 로고    scopus 로고
    • Identification of factors impeding the production of a single-chain antibody fragment in Escherichia coli by comparing in vivo and in vitro expression
    • Oelschlaeger, S. Lange, J. Schmitt, M. Siemann, M. Reuss, and R.D. Schmid Identification of factors impeding the production of a single-chain antibody fragment in Escherichia coli by comparing in vivo and in vitro expression Appl. Microbiol. Biotechnol. 61 2003 123 132
    • (2003) Appl. Microbiol. Biotechnol. , vol.61 , pp. 123-132
    • Oelschlaeger1    Lange, S.2    Schmitt, J.3    Siemann, M.4    Reuss, M.5    Schmid, R.D.6
  • 22
    • 0019737171 scopus 로고
    • L-Asparaginase: Discovery and development as a tumor-inhibitory agent
    • J.D. Broome l-Asparaginase: discovery and development as a tumor-inhibitory agent Cancer Treat. Rep. 65 1981 111 114
    • (1981) Cancer Treat. Rep. , vol.65 , pp. 111-114
    • Broome, J.D.1
  • 24
    • 0014298774 scopus 로고
    • Studies on the mechanism of tumor inhibition by l-asparaginase
    • J.D. Broome Studies on the mechanism of tumor inhibition by l-asparaginase J. Exp. Med. 127 1968 1055 1072
    • (1968) J. Exp. Med. , vol.127 , pp. 1055-1072
    • Broome, J.D.1
  • 25
  • 26
    • 0013971104 scopus 로고
    • Two l-asparaginases from E. coli and their action against tumors
    • J.H. Schwartz, J.Y. Reeves, and J.D. Broome Two l-asparaginases from E. coli and their action against tumors Proc. Natl. Acad. Sci. USA 56 1966 1516 1519
    • (1966) Proc. Natl. Acad. Sci. USA , vol.56 , pp. 1516-1519
    • Schwartz, J.H.1    Reeves, J.Y.2    Broome, J.D.3
  • 27
    • 0013837631 scopus 로고
    • Antilymphoma activity of l-asparaginase in vivo: Clearance rates of enzyme preparations from guinea pig serum and yeast in relation to their effect on tumor growth
    • J.D. Broome Antilymphoma activity of l-asparaginase in vivo: clearance rates of enzyme preparations from guinea pig serum and yeast in relation to their effect on tumor growth J. Natl. Cancer Inst. 35 1965 967 974
    • (1965) J. Natl. Cancer Inst. , vol.35 , pp. 967-974
    • Broome, J.D.1
  • 28
    • 0027530947 scopus 로고
    • Crystal structure of Escherichia coli l-asparaginase, an enzyme used in cancer therapy
    • A.L. Swain, M. Jaskolski, D. Housset, J.K. Rao, and A. Wlodawer Crystal structure of Escherichia coli l-asparaginase, an enzyme used in cancer therapy Proc. Natl. Acad. Sci. USA 90 1993 1474 1478
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1474-1478
    • Swain, A.L.1    Jaskolski, M.2    Housset, D.3    Rao, J.K.4    Wlodawer, A.5
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 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.1
  • 31
    • 0015240503 scopus 로고
    • L-Asparaginase from Escherichia coli B. Physicochemical studies of the dissociation process
    • S. Shifrin, S.W. Luborsky, and B.J. Grochowski l-Asparaginase from Escherichia coli B. Physicochemical studies of the dissociation process J. Biol. Chem. 246 1971 7708 7714
    • (1971) J. Biol. Chem. , vol.246 , pp. 7708-7714
    • Shifrin, S.1    Luborsky, S.W.2    Grochowski, B.J.3
  • 32
    • 0036192267 scopus 로고    scopus 로고
    • Growth rate-dependent changes in Escherichia coli membrane structure and protein leakage
    • A. Shokri, A.M. Sanden, and G. Larsson Growth rate-dependent changes in Escherichia coli membrane structure and protein leakage Appl. Microbiol. Biotechnol. 58 2002 386 392
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 386-392
    • Shokri, A.1    Sanden, A.M.2    Larsson, G.3
  • 33
    • 0346725824 scopus 로고    scopus 로고
    • Stationary phase protein overproduction is a fundamental capability of Escherichia coli
    • Ou, L. Wang, X. Ding, J. Du, Y. Zhang, H. Chen, and A. Xu Stationary phase protein overproduction is a fundamental capability of Escherichia coli Biochem. Biophys. Res. Commun. 314 2004 174 180
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 174-180
    • Ou1    Wang, L.2    Ding, X.3    Du, J.4    Zhang, Y.5    Chen, H.6    Xu, A.7
  • 34
    • 0037338060 scopus 로고    scopus 로고
    • Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase
    • C.A. Galloway, M.P. Sowden, and H.C. Smith Increasing the yield of soluble recombinant protein expressed in E. coli by induction during late log phase Biotechniques 34 2003 524 526
    • (2003) Biotechniques , vol.34 , pp. 524-526
    • Galloway, C.A.1    Sowden, M.P.2    Smith, H.C.3
  • 35
    • 0026135121 scopus 로고
    • Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts
    • E. Harms, A. Wehner, M.P. Jennings, K.J. Pugh, I.R. Beacham, and K.H. Rohm Construction of expression systems for Escherichia coli asparaginase II and two-step purification of the recombinant enzyme from periplasmic extracts Protein Express. Purif. 2 1991 144 150
    • (1991) Protein Express. Purif. , vol.2 , pp. 144-150
    • Harms, E.1    Wehner, A.2    Jennings, M.P.3    Pugh, K.J.4    Beacham, I.R.5    Rohm, K.H.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.