메뉴 건너뛰기




Volumn 42, Issue 8, 2007, Pages 1259-1263

Activity of recombinant GST in Escherichia coli grown on glucose and glycerol

Author keywords

Activity; E. coli; Glutathione S transferase; Glycerol

Indexed keywords

CARBON SOURCES; CELL LYSIS; GLUTATHIONE-S-TRANSFERASE (GST); SUPERNATANT;

EID: 34447628052     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2007.05.022     Document Type: Article
Times cited : (10)

References (21)
  • 1
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: biological role of inclusion bodies
    • Villaverde A., and Carrió M.M. Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 25 (2003) 1385-1395
    • (2003) Biotechnol Lett , vol.25 , pp. 1385-1395
    • Villaverde, A.1    Carrió, M.M.2
  • 2
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimising heterologous protein expression in Escherichia coli
    • Hannig G., and Makrides S.C. Strategies for optimising 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
  • 3
    • 0027212498 scopus 로고
    • Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins
    • Frangioni J.V., and Neel B.G. Solubilization and purification of enzymatically active glutathione S-transferase (pGEX) fusion proteins. Anal Biochem 210 (1993) 179-187
    • (1993) Anal Biochem , vol.210 , pp. 179-187
    • Frangioni, J.V.1    Neel, B.G.2
  • 4
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures
    • Gekko K., and Timasheff S.N. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20 (1981) 4667-4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 5
    • 0026534357 scopus 로고
    • Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol
    • Sawano H., Koumoto Y., Ohta K., Sasaki Y., Segewa S., and Tachibana H. Efficient in vitro folding of the three-disulfide derivatives of hen lysozyme in the presence of glycerol. FEBS Lett 303 (1992) 11-14
    • (1992) FEBS Lett , vol.303 , pp. 11-14
    • Sawano, H.1    Koumoto, Y.2    Ohta, K.3    Sasaki, Y.4    Segewa, S.5    Tachibana, H.6
  • 6
    • 0032755251 scopus 로고    scopus 로고
    • Manipulating the amyloid-β aggregation pathway with chemical chaperones
    • Yang D.-S., Yip C.M., Huang T.H.J., Chakrabartty A., and Fraser P.E. Manipulating the amyloid-β aggregation pathway with chemical chaperones. J Biol Chem 274 (1999) 32970-32974
    • (1999) J Biol Chem , vol.274 , pp. 32970-32974
    • Yang, D.-S.1    Yip, C.M.2    Huang, T.H.J.3    Chakrabartty, A.4    Fraser, P.E.5
  • 7
    • 0025753565 scopus 로고
    • Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli
    • Strandberg L., and Enfors S.-O. Factors influencing inclusion body formation in the production of a fused protein in Escherichia coli. Appl Environ Microbiol 57 (1991) 1669-1674
    • (1991) Appl Environ Microbiol , vol.57 , pp. 1669-1674
    • Strandberg, L.1    Enfors, S.-O.2
  • 8
    • 0034978522 scopus 로고    scopus 로고
    • Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system
    • Leandro P., Lechner M.C., de Almeida I.T., and Konecki D. Glycerol increases the yield and activity of human phenylalanine hydroxylase mutant enzymes produced in a prokaryotic expression system. Mol Gen Metabol 73 (2001) 173-178
    • (2001) Mol Gen Metabol , vol.73 , pp. 173-178
    • Leandro, P.1    Lechner, M.C.2    de Almeida, I.T.3    Konecki, D.4
  • 9
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • Sato S., Ward C.L., Krouse M.E., Wine J.J., and Kopito R.R. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J Biol Chem 271 (1996) 635-638
    • (1996) J Biol Chem , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 10
    • 0025123399 scopus 로고
    • Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli
    • Bowden G.A., and Georgiou G. Folding and aggregation of β-lactamase in the periplasmic space of Escherichia coli. J Biol Chem 265 (1990) 16760-16766
    • (1990) J Biol Chem , vol.265 , pp. 16760-16766
    • Bowden, G.A.1    Georgiou, G.2
  • 11
    • 0026327753 scopus 로고
    • A novel strategy for production of a highly expressed recombinant protein in an active form
    • Blackwell J.R., and Horgan R. A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS Lett 295 (1991) 10-12
    • (1991) FEBS Lett , vol.295 , pp. 10-12
    • Blackwell, J.R.1    Horgan, R.2
  • 12
    • 33748588165 scopus 로고    scopus 로고
    • Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant
    • Ignatova Z., and Gierasch L.M. Inhibition of protein aggregation in vitro and in vivo by a natural osmoprotectant. Proc Natl Acad Sci 103 (2006) 13357-13361
    • (2006) Proc Natl Acad Sci , vol.103 , pp. 13357-13361
    • Ignatova, Z.1    Gierasch, L.M.2
  • 13
    • 0035813451 scopus 로고    scopus 로고
    • Automatic inducer addition and harvesting of recombinant Escherichia coli cultures based on indirect on-line estimation of biomass concentration and specific growth rate
    • Eriksen N.T., Kratchmarova I., Neve S., Kristiansen K., and Iversen J.J.L. Automatic inducer addition and harvesting of recombinant Escherichia coli cultures based on indirect on-line estimation of biomass concentration and specific growth rate. Biotechnol Bioeng 75 (2001) 355-361
    • (2001) Biotechnol Bioeng , vol.75 , pp. 355-361
    • Eriksen, N.T.1    Kratchmarova, I.2    Neve, S.3    Kristiansen, K.4    Iversen, J.J.L.5
  • 15
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature
    • Schein C.H., and Noteborn M.H.M. Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Bio/Technol 6 (1988) 291-294. http://www.nature.com/nbt/journal/v6/n3/abs/nbt0388-291.html
    • (1988) Bio/Technol , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method or the quantification of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. A rapid and sensitive method or the quantification 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
    • 0037009261 scopus 로고    scopus 로고
    • Growth and proton exchange in recombinant Escherichia coli BL21
    • Christensen M.L., and Eriksen N.T. Growth and proton exchange in recombinant Escherichia coli BL21. Enzyme Microb Technol 31 (2002) 566-574
    • (2002) Enzyme Microb Technol , vol.31 , pp. 566-574
    • Christensen, M.L.1    Eriksen, N.T.2
  • 19
    • 0025264582 scopus 로고
    • Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations
    • Luli G.W., and Strohl W.R. Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations. Appl Environ Microbiol 56 (1990) 1004-1011
    • (1990) Appl Environ Microbiol , vol.56 , pp. 1004-1011
    • Luli, G.W.1    Strohl, W.R.2
  • 20
    • 15844395096 scopus 로고    scopus 로고
    • Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins
    • Thomas J.G., and Banyez F. Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins. J Biol Chem 271 (1996) 11141-11147
    • (1996) J Biol Chem , vol.271 , pp. 11141-11147
    • Thomas, J.G.1    Banyez, F.2
  • 21
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding in protein folding and aggregation
    • van den Berg B., Ellis R.J., and Dobson C.M. Effects of macromolecular crowding in protein folding and aggregation. EMBO J 18 (1999) 6927-6933
    • (1999) EMBO J , vol.18 , pp. 6927-6933
    • van den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.