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Volumn 9, Issue 3, 2006, Pages 291-296

Production of recombinant enzymes of wide use for research

Author keywords

Bioactivity; Protein expression; Purification; Recombinant enzymes

Indexed keywords

ENZYMES; MOLECULAR STRUCTURE; PROTEINS; PURIFICATION;

EID: 33745833005     PISSN: 07173458     EISSN: 07173458     Source Type: Journal    
DOI: 10.2225/vol9-issue3-16     Document Type: Article
Times cited : (9)

References (17)
  • 1
    • 0035810768 scopus 로고    scopus 로고
    • Autoradiographic localization of angiotensin II receptors in developing rat cerebellum and brainstem
    • ARCE, M.E.; SANCHEZ, S.; SELTZER, A. and CIUFFO, G.M. Autoradiographic localization of angiotensin II receptors in developing rat cerebellum and brainstem. Regulatory Peptides, 2001, vol. 99, no. 1, p. 53-60.
    • (2001) Regulatory Peptides , vol.99 , Issue.1 , pp. 53-60
    • Arce, M.E.1    Sanchez, S.2    Seltzer, A.3    Ciuffo, G.M.4
  • 4
    • 14744269790 scopus 로고
    • Structure and morphology of protein inclusion bodies in E. coli
    • BOWDEN, G.A.; PAREDES, A.M. and GEORGIOU, G. Structure and morphology of protein inclusion bodies in E. coli. Bio/Technology, 1991, vol. 9, p. 725-730.
    • (1991) Bio/Technology , vol.9 , pp. 725-730
    • Bowden, G.A.1    Paredes, A.M.2    Georgiou, G.3
  • 5
    • 0026557995 scopus 로고
    • Inclusion bodies of the thermophillic endoglucanase D from Clostridium thermocellium are made of native enzyme that resist 8M urea
    • CHAFFOTTE, A.F.; GUILLOU, Y. and GOLDBERG, M.E. Inclusion bodies of the thermophillic endoglucanase D from Clostridium thermocellium are made of native enzyme that resist 8M urea. European Journal of Biochemistry, 1992, vol. 205, p. 369-373.
    • (1992) European Journal of Biochemistry , vol.205 , pp. 369-373
    • Chaffotte, A.F.1    Guillou, Y.2    Goldberg, M.E.3
  • 8
    • 0025633829 scopus 로고
    • Purification of Thermus aquaticus DNA polymerase expressed in Escherichia coli
    • ENGELKE, D.R.; KRISKOS, A.; BRUCK, M.E. and GINSBURG, D. Purification of Thermus aquaticus DNA polymerase expressed in Escherichia coli. Analytical Biochemistry, 1990, vol. 191, no. 2, p. 396-400.
    • (1990) Analytical Biochemistry , vol.191 , Issue.2 , pp. 396-400
    • Engelke, D.R.1    Kriskos, A.2    Bruck, M.E.3    Ginsburg, D.4
  • 9
    • 0024560060 scopus 로고
    • Isolation, characterization, and expression in Escherichia coli of the DNA polymerase gene from Thermus aquaticus
    • LAWYER, F.C.; STOFFEL, S.; SAIKI, R.K.; MYAMBO, K.; DRUMMOND, R. and GELFAND, D.H. Isolation, characterization, and expression in Escherichia coli of the DNA polymerase gene from Thermus aquaticus. Journal of Biological Chemistry, 1989, vol. 264, no. 11, p. 6427-6437.
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.11 , pp. 6427-6437
    • Lawyer, F.C.1    Stoffel, S.2    Saiki, R.K.3    Myambo, K.4    Drummond, R.5    Gelfand, D.H.6
  • 10
    • 0031023734 scopus 로고    scopus 로고
    • Upregulation of vascular Angiotensin II receptor gene expression by lowdensity lipoprotein in vascular smooth muscle cells
    • NICKENIG, G.; SACHINIDIS, A.; MICHAELSEN, F.; BOHM, M.; SEEWALD, S.; VETTER, H. Upregulation of vascular Angiotensin II receptor gene expression by lowdensity lipoprotein in vascular smooth muscle cells. Circulation, 1997, vol. 95, no. 2, p. 473-478.
    • (1997) Circulation , vol.95 , Issue.2 , pp. 473-478
    • Nickenig, G.1    Sachinidis, A.2    Michaelsen, F.3    Bohm, M.4    Seewald, S.5    Vetter, H.6
  • 11
    • 33745850540 scopus 로고    scopus 로고
    • Rapid purification of high activity Taq DNA polymerase expressed in transformed E. coli cells
    • OTTINO, P. Rapid purification of high activity Taq DNA polymerase expressed in transformed E. coli cells. Transactions of the Zimbabwe Scientific Association, 1998, vol. 72, p. 23-26.
    • (1998) Transactions of the Zimbabwe Scientific Association , vol.72 , pp. 23-26
    • Ottino, P.1
  • 14
    • 0027527885 scopus 로고
    • Rapid purification of high-activity Taq DNA polymerase
    • PLUTHERO, F.G. Rapid purification of high-activity Taq DNA polymerase. Nucleic Acids Research, 1993, vol. 21, no. 20, p. 4850-4851.
    • (1993) Nucleic Acids Research , vol.21 , Issue.20 , pp. 4850-4851
    • Pluthero, F.G.1
  • 15
    • 0031854137 scopus 로고    scopus 로고
    • Cloning, expression, and purification of a catalytic fragment of Moloney murine leukaemia virus reverse transcriptase: Crystallization of nucleic acid complexes
    • SUN, D.; JESSEN, S.; LIU, C.; LIU, X; NAJMUDIN, S. and GEORGIADIS, M.M. Cloning, expression, and purification of a catalytic fragment of Moloney murine leukaemia virus reverse transcriptase: Crystallization of nucleic acid complexes. Protein Science, 1998, vol. 7, no. 7, p. 1575-1582.
    • (1998) Protein Science , vol.7 , Issue.7 , pp. 1575-1582
    • Sun, D.1    Jessen, S.2    Liu, C.3    Liu, X.4    Najmudin, S.5    Georgiadis, M.M.6
  • 16
    • 0032007545 scopus 로고    scopus 로고
    • Reverse transcriptase of mouse mammary tumour virus: Expression in bacteria, purification and biochemical characterization
    • TAUBE, R.; LOYA, S.; VIDAN, O.A.; PERACH, M. and HIZI, A. Reverse transcriptase of mouse mammary tumour virus: expression in bacteria, purification and biochemical characterization. Biochemical Journal, 1998, vol. 329, no. 3, p. 579-587.
    • (1998) Biochemical Journal , vol.329 , Issue.3 , pp. 579-587
    • Taube, R.1    Loya, S.2    Vidan, O.A.3    Perach, M.4    Hizi, A.5
  • 17
    • 0002432883 scopus 로고
    • Protein folding in biotechnology
    • PAIN, R.H. ed. Oxford University Press
    • THATCHER, D.R. and HITCHCOCK, A. Protein folding in biotechnology. In: PAIN, R.H. ed. Mechanism of Protein Folding. Oxford University Press, 1994. p. 229-261.
    • (1994) Mechanism of Protein Folding , pp. 229-261
    • Thatcher, D.R.1    Hitchcock, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.