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Volumn 21, Issue 6, 1998, Pages 275-282

Generation of a histidine-tagged antibotulinum toxin antibody fragment in E. coli: Effects of post-induction temperature on yield and IMAC binding-affinity

Author keywords

Botulinum toxin; E. coli fermentation; Fab antibody expression; Immobilized metal affinity chromatography (IMAC); Proteases; Temperature sensitivity

Indexed keywords

BOTULINUM ANTISERUM; BOTULINUM TOXIN; HISTIDINE; IMMUNOGLOBULIN F(AB) FRAGMENT; ISOPROPYL THIOGALACTOSIDE; PROTEINASE; RECOMBINANT ANTIBODY; SIGNAL PEPTIDE;

EID: 0032458558     PISSN: 13675435     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.jim.2900577     Document Type: Article
Times cited : (6)

References (23)
  • 3
    • 0030596493 scopus 로고    scopus 로고
    • Directing antigen specificity towards botulinum neurotoxin with combinatorial phage display libraries
    • 3 Emanuel P, T O'Brien, J Burans, BR DasGupta, JJ Valdes and M Eldefrawi. 1996. Directing antigen specificity towards botulinum neurotoxin with combinatorial phage display libraries. J Immunol Meth 193: 189-197.
    • (1996) J Immunol Meth , vol.193 , pp. 189-197
    • Emanuel, P.1    O'Brien, T.2    Burans, J.3    DasGupta, B.R.4    Valdes, J.J.5    Eldefrawi, M.6
  • 4
    • 0013567056 scopus 로고
    • Release of periplasmic enzymes and other physiological effects of β-lactamase overproduction in Escherichia coli by manipulation of culture conditions
    • 4 Georgiou G, ML Shuler and DB Wilson. 1988. Release of periplasmic enzymes and other physiological effects of β-lactamase overproduction in Escherichia coli by manipulation of culture conditions. J Ferment Bioeng 69: 159-165.
    • (1988) J Ferment Bioeng , vol.69 , pp. 159-165
    • Georgiou, G.1    Shuler, M.L.2    Wilson, D.B.3
  • 5
    • 0022344755 scopus 로고
    • Production of abnormal proteins in E. Coli stimulates transcription of Ion and other heat shock dependent genes
    • 5 Goff SA and AL Goldberg. 1985. Production of abnormal proteins in E. coli stimulates transcription of Ion and other heat shock dependent genes. Cell 41: 587-595.
    • (1985) Cell , vol.41 , pp. 587-595
    • Goff, S.A.1    Goldberg, A.L.2
  • 6
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energy-dependent proteases and their targets
    • 6 Gottesman S and M Maurizi. 1992. Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol Rev 56: 592-621.
    • (1992) Microbiol Rev , vol.56 , pp. 592-621
    • Gottesman, S.1    Maurizi, M.2
  • 7
    • 0027909877 scopus 로고
    • Response dynamics of 26, 34, 39, 54, and 80 kDa proteases in induced cultures of recombinant Escherichia coli
    • 7 Harcum SW and WE Bentley. 1993. Response dynamics of 26, 34, 39, 54, and 80 kDa proteases in induced cultures of recombinant Escherichia coli. Biotechnol Bioengin 42: 675-685.
    • (1993) Biotechnol Bioengin , vol.42 , pp. 675-685
    • Harcum, S.W.1    Bentley, W.E.2
  • 8
    • 8044237717 scopus 로고    scopus 로고
    • High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions
    • 8 Horn U, W Strittmatter, A Krebber, U Knüpfer, M Kujau, R Wenderoth, K Müller, S Matzku, A Plückthun and D Riesenberg. 1996. High volumetric yields of functional dimeric miniantibodies in Escherichia coli, using an optimized expression vector and high-cell-density fermentation under non-limited growth conditions. Appl Microbiol Biotechnol 46: 524-532.
    • (1996) Appl Microbiol Biotechnol , vol.46 , pp. 524-532
    • Horn, U.1    Strittmatter, W.2    Krebber, A.3    Knüpfer, U.4    Kujau, M.5    Wenderoth, R.6    Müller, K.7    Matzku, S.8    Plückthun, A.9    Riesenberg, D.10
  • 9
    • 0023117045 scopus 로고
    • Intracellular degradation of proteins in relation to their location in Escherichia coli cells
    • 9 Kitano K, S Fugimoto, M Nakao, T Watanabe and Y Nakao. 1987. Intracellular degradation of proteins in relation to their location in Escherichia coli cells. J Biotechnol 5: 77-86.
    • (1987) J Biotechnol , vol.5 , pp. 77-86
    • Kitano, K.1    Fugimoto, S.2    Nakao, M.3    Watanabe, T.4    Nakao, Y.5
  • 10
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • 10 Knappik A and A Plückthun. 1995. Engineered turns of a recombinant antibody improve its in vivo folding. Protein Eng 8: 81-89.
    • (1995) Protein Eng , vol.8 , pp. 81-89
    • Knappik, A.1    Plückthun, A.2
  • 11
    • 0026645163 scopus 로고
    • Proteolytic response to the expression of an abnormal β-galactosidase in Escherichia coli
    • 11 Kosinski M, U Rinas and J Bailey. 1992. Proteolytic response to the expression of an abnormal β-galactosidase in Escherichia coli. Appl Microbiol Biotechnol 37: 335-341.
    • (1992) Appl Microbiol Biotechnol , vol.37 , pp. 335-341
    • Kosinski, M.1    Rinas, U.2    Bailey, J.3
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage
    • 12 Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 13
    • 0024316280 scopus 로고
    • Peptidases and proteases of Escherichia coli and Salmonella typhimurium
    • 13 Lazdunski AM. 1989. Peptidases and proteases of Escherichia coli and Salmonella typhimurium. FEMS Microbiol Rev 63: 265-276.
    • (1989) FEMS Microbiol Rev , vol.63 , pp. 265-276
    • Lazdunski, A.M.1
  • 14
    • 0026601663 scopus 로고
    • Protease and protein degradation in Escherichia coli
    • 14 Maurizi M. 1992. Protease and protein degradation in Escherichia coli. Experientia 48: 178-199.
    • (1992) Experientia , vol.48 , pp. 178-199
    • Maurizi, M.1
  • 15
    • 0021693955 scopus 로고
    • Genetics and regulation of heat shock proteins
    • 15 Neidhardt F, R VanBogelan and V Vaughn. 1984. Genetics and regulation of heat shock proteins. Ann Rev Genet 18: 295-329.
    • (1984) Ann Rev Genet , vol.18 , pp. 295-329
    • Neidhardt, F.1    VanBogelan, R.2    Vaughn, V.3
  • 16
    • 0020490526 scopus 로고
    • Purification and characterization of two novel proteolytic enzymes in membranes of E. Coli
    • 16 Pacaud M. 1982. Purification and characterization of two novel proteolytic enzymes in membranes of E. coli. J Biol Chem 257: 4333-4339.
    • (1982) J Biol Chem , vol.257 , pp. 4333-4339
    • Pacaud, M.1
  • 18
    • 14744276972 scopus 로고
    • Antibody engineering: Advances from the use of E. Coli expression systems
    • 18 Plückthun A. 1991. Antibody engineering: advances from the use of E. coli expression systems. Bio/Technology 9: 545-551.
    • (1991) Bio/Technology , vol.9 , pp. 545-551
    • Plückthun, A.1
  • 19
    • 0016717761 scopus 로고
    • Metal chelate affinity chromatography, a new approach to protein fractionation
    • 19 Porath J, J Carlsson, I Olsson and G Belfrage. 1975. Metal chelate affinity chromatography, a new approach to protein fractionation. Nature 258: 598-599.
    • (1975) Nature , vol.258 , pp. 598-599
    • Porath, J.1    Carlsson, J.2    Olsson, I.3    Belfrage, G.4
  • 20
    • 85038178043 scopus 로고    scopus 로고
    • PhD dissertation. University of Maryland, College Park
    • 20 Pulliam-Holoman T. 1996. PhD dissertation. University of Maryland, College Park.
    • (1996)
    • Pulliam-Holoman, T.1
  • 21
    • 0029636928 scopus 로고
    • Fed-batch feeding and induction policies that improve foreign protein synthesis and stability by avoiding stress responses
    • 21 Ramirez DM and WE Bentley. 1995. Fed-batch feeding and induction policies that improve foreign protein synthesis and stability by avoiding stress responses. Biotechnol Bioengin 47: 596-609.
    • (1995) Biotechnol Bioengin , vol.47 , pp. 596-609
    • Ramirez, D.M.1    Bentley, W.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.