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Volumn 1764, Issue 4, 2006, Pages 793-799

Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy

Author keywords

FT IR spectroscopy; Heterologous protein production; Human growth hormone; Inclusion bodies; Interferon alpha; Protein aggregation

Indexed keywords

CELL PROTEIN; RECOMBINANT ALPHA2B INTERFERON; RECOMBINANT GROWTH HORMONE;

EID: 33646589053     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.12.005     Document Type: Article
Times cited : (115)

References (30)
  • 1
    • 0028260192 scopus 로고
    • Native-like secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR
    • Oberg K., Chrunyk B.A., Wetzel R., and Fink A.L. Native-like secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. Biochemistry 33 (1994) 2628-2634
    • (1994) Biochemistry , vol.33 , pp. 2628-2634
    • Oberg, K.1    Chrunyk, B.A.2    Wetzel, R.3    Fink, A.L.4
  • 2
    • 0028057034 scopus 로고
    • Secondary structure characterization of beta-lactamase inclusion bodies
    • Przybycien T.M., Dunn J.P., Valax P., and Georgiou G. Secondary structure characterization of beta-lactamase inclusion bodies. Protein Eng. 7 (1994) 131-136
    • (1994) Protein Eng. , vol.7 , pp. 131-136
    • Przybycien, T.M.1    Dunn, J.P.2    Valax, P.3    Georgiou, G.4
  • 3
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: folding aggregates, inclusion bodies and amyloid
    • Fink A.L. Protein aggregation: folding aggregates, inclusion bodies and amyloid. Fold Des. 3 (1998) 9-23
    • (1998) Fold Des. , vol.3 , pp. 9-23
    • Fink, A.L.1
  • 4
    • 1642491754 scopus 로고    scopus 로고
    • Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins
    • Umetsu M., Tsumoto K., Ashish K., Nitta S., Tanaka Y., Adschiri T., and Kumagai I. Structural characteristics and refolding of in vivo aggregated hyperthermophilic archaeon proteins. FEBS Lett. 557 (2004) 49-56
    • (2004) FEBS Lett. , vol.557 , pp. 49-56
    • Umetsu, M.1    Tsumoto, K.2    Ashish, K.3    Nitta, S.4    Tanaka, Y.5    Adschiri, T.6    Kumagai, I.7
  • 5
    • 20444363444 scopus 로고    scopus 로고
    • Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    • Ami D., Natalello A., Gatti-Lafranconi P., Lotti M., and Doglia S.M. Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Lett. 579 (2005) 3433-3436
    • (2005) FEBS Lett. , vol.579 , pp. 3433-3436
    • Ami, D.1    Natalello, A.2    Gatti-Lafranconi, P.3    Lotti, M.4    Doglia, S.M.5
  • 7
    • 0034105491 scopus 로고    scopus 로고
    • Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli
    • Patra A.K., Mukhopadhyay R., Mukhija R., Krishnan A., Garg L.C., and Panda A.K. Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli. Protein Expression Purif. 18 (2000) 182-192
    • (2000) Protein Expression Purif. , vol.18 , pp. 182-192
    • Patra, A.K.1    Mukhopadhyay, R.2    Mukhija, R.3    Krishnan, A.4    Garg, L.C.5    Panda, A.K.6
  • 8
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh S.M., and Panda A.K. Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 99 (2005) 303-310
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 10
    • 0025921901 scopus 로고
    • High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D
    • Tokatlidis K., Dhurjati P., Millet J., Beguin P., and Aubert J.P. High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. FEBS Lett. 282 (1991) 205-208
    • (1991) FEBS Lett. , vol.282 , pp. 205-208
    • Tokatlidis, K.1    Dhurjati, P.2    Millet, J.3    Beguin, P.4    Aubert, J.P.5
  • 11
    • 0344395589 scopus 로고    scopus 로고
    • FT-IR study of heterologous protein expression in recombinant Escherichia coli strains
    • Ami D., Bonecchi L., Calì S., Orsini G., Tonon G., and Doglia S.M. FT-IR study of heterologous protein expression in recombinant Escherichia coli strains. Biochim. Biophys. Acta 1624 (2003) 6-10
    • (2003) Biochim. Biophys. Acta , vol.1624 , pp. 6-10
    • Ami, D.1    Bonecchi, L.2    Calì, S.3    Orsini, G.4    Tonon, G.5    Doglia, S.M.6
  • 13
    • 33646550770 scopus 로고    scopus 로고
    • M. Vanoni, P. Tortora, G. Tonon, G. Taylor, G. Orsini. Novel soluble endoprotease for the in vitro processing of recombinant proteins, International patent application (2001) (PCT/EPO1/13257).
  • 16
    • 0028062558 scopus 로고
    • Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy
    • Microscopy, Optical Spectroscopy, and Macroscopic Techniques. Jones C., Mulloy B., and Thomas A.H. (Eds), Humana Press, Totowa, NJ
    • Haris P.I., and Chapman D. Analysis of polypeptide and protein structures using Fourier transform infrared spectroscopy. In: Jones C., Mulloy B., and Thomas A.H. (Eds). Microscopy, Optical Spectroscopy, and Macroscopic Techniques. Methods in Molecular Biology vol. 22 (1994), Humana Press, Totowa, NJ 183-202
    • (1994) Methods in Molecular Biology , vol.22 , pp. 183-202
    • Haris, P.I.1    Chapman, D.2
  • 17
    • 12844274977 scopus 로고    scopus 로고
    • Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy
    • Natalello A., Ami D., Brocca S., Lotti M., and Doglia S.M. Secondary structure, conformational stability and glycosylation of a recombinant Candida rugosa lipase studied by Fourier-transform infrared spectroscopy. Biochem. J. 385 (2005) 511-517
    • (2005) Biochem. J. , vol.385 , pp. 511-517
    • Natalello, A.1    Ami, D.2    Brocca, S.3    Lotti, M.4    Doglia, S.M.5
  • 18
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi H., and Byler D.M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 130 (1986) 291-311
    • (1986) Methods Enzymol. , vol.130 , pp. 291-311
    • Susi, H.1    Byler, D.M.2
  • 19
    • 0032818805 scopus 로고    scopus 로고
    • FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media
    • Haris P.I., and Severcan F. FTIR spectroscopic characterization of protein structure in aqueous and non-aqueous media. J. Mol. Catal., B Enzym. 7 (1999) 207-221
    • (1999) J. Mol. Catal., B Enzym. , vol.7 , pp. 207-221
    • Haris, P.I.1    Severcan, F.2
  • 20
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • Goormaghtigh E., Raussens V., and Ruysschaert JM. Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes. Biochim. Biophys. Acta 1422 (1999) 105-185
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, JM.3
  • 21
    • 0032831759 scopus 로고    scopus 로고
    • Fourier transform infrared spectroscopy in analysis of protein deposits
    • Seshadri S., Khurana R., and Fink A.L. Fourier transform infrared spectroscopy in analysis of protein deposits. Methods Enzymol. 309 (1999) 559-576
    • (1999) Methods Enzymol. , vol.309 , pp. 559-576
    • Seshadri, S.1    Khurana, R.2    Fink, A.L.3
  • 22
    • 0033047392 scopus 로고    scopus 로고
    • Use of infrared spectroscopy to assess secondary structure of human growth hormone within biodegradable microspheres
    • Yang T.H., Dong A., Meyer J., Johnson O.L., Cleland J.L., and Carpenter J.F. Use of infrared spectroscopy to assess secondary structure of human growth hormone within biodegradable microspheres. J. Pharm. Sci. 88 (1999) 161-165
    • (1999) J. Pharm. Sci. , vol.88 , pp. 161-165
    • Yang, T.H.1    Dong, A.2    Meyer, J.3    Johnson, O.L.4    Cleland, J.L.5    Carpenter, J.F.6
  • 23
    • 0032970303 scopus 로고    scopus 로고
    • On the structural preservation of recombinant human growth hormone in a dried film of a synthetic biodegradable polymer
    • Carrasquillo K.G., Costantino H.R., Cordero R.A., Hsu C.C., and Griebenow K. On the structural preservation of recombinant human growth hormone in a dried film of a synthetic biodegradable polymer. J. Pharm. Sci. 88 (1999) 166-173
    • (1999) J. Pharm. Sci. , vol.88 , pp. 166-173
    • Carrasquillo, K.G.1    Costantino, H.R.2    Cordero, R.A.3    Hsu, C.C.4    Griebenow, K.5
  • 24
    • 0031402313 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins and peptides in lipid bilayers
    • Tamm L.K., and Tatulian S.A. Infrared spectroscopy of proteins and peptides in lipid bilayers. Q. Rev. Biophys. 304 (1997) 365-429
    • (1997) Q. Rev. Biophys. , vol.304 , pp. 365-429
    • Tamm, L.K.1    Tatulian, S.A.2
  • 25
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo J.L.R., and Goni F.M. Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog. Biophys. Mol. Biol. 72 (1999) 367-405
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goni, F.M.2
  • 27
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • Schrodel A., and de Marco A. Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem. 6 (2005) 10
    • (2005) BMC Biochem. , vol.6 , pp. 10
    • Schrodel, A.1    de Marco, A.2
  • 30
    • 0142040121 scopus 로고    scopus 로고
    • Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein
    • Sokolowski F., Modler A.J., Masuch R., Zirwer D., Baier M., Lutsch G., Moss D.A., Gast K., and Naumann D. Formation of critical oligomers is a key event during conformational transition of recombinant Syrian hamster prion protein. J. Biol. Chem. 278 (2003) 40481-40492
    • (2003) J. Biol. Chem. , vol.278 , pp. 40481-40492
    • Sokolowski, F.1    Modler, A.J.2    Masuch, R.3    Zirwer, D.4    Baier, M.5    Lutsch, G.6    Moss, D.A.7    Gast, K.8    Naumann, D.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.