메뉴 건너뛰기




Volumn 87, Issue 9, 1998, Pages 1069-1076

Aggregation of recombinant human interferon gamma: Kinetics and structural transitions

Author keywords

[No Author keywords available]

Indexed keywords

RECOMBINANT GAMMA INTERFERON;

EID: 0031684574     PISSN: 00223549     EISSN: None     Source Type: Journal    
DOI: 10.1021/js9801384     Document Type: Article
Times cited : (159)

References (40)
  • 1
    • 0029785453 scopus 로고    scopus 로고
    • Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
    • Speed, M. A.; Wang, D. I. C.; King, J. Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition. Nat. Biotechnol. 1996, 14, 1283-1287.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 2
    • 0031127778 scopus 로고    scopus 로고
    • Construction and overexpression of a synthetic gene for human DNA methylguanine methyltransferase: Renaturation and rapid purification of the protein
    • Brown, L. R.; Deng, J.; Noll, D. M.; Mori, N.; Clarke, N. D. Construction and overexpression of a synthetic gene for human DNA methylguanine methyltransferase: renaturation and rapid purification of the protein. Protein. Expr. Purif. 1997, 9, 337-45.
    • (1997) Protein. Expr. Purif. , vol.9 , pp. 337-345
    • Brown, L.R.1    Deng, J.2    Noll, D.M.3    Mori, N.4    Clarke, N.D.5
  • 3
    • 0030991899 scopus 로고    scopus 로고
    • Roles of histidine 31 and tryptophan 34 in the structure, self-association, and folding of murine interleukin-6
    • Matthews, J. M.; Ward, L. D.; Hammacher, A.; Norton, R. S.; Simpson, R. J. Roles of histidine 31 and tryptophan 34 in the structure, self-association, and folding of murine interleukin-6. Biochemistry 1997, 36, 6187-96.
    • (1997) Biochemistry , vol.36 , pp. 6187-6196
    • Matthews, J.M.1    Ward, L.D.2    Hammacher, A.3    Norton, R.S.4    Simpson, R.J.5
  • 4
    • 0029653845 scopus 로고
    • Folding and association versus misfolding and aggregation of proteins
    • Jaenicke, R. Folding and association versus misfolding and aggregation of proteins. Philos. Trans. R. Soc. London B 1995, 348, 97-105.
    • (1995) Philos. Trans. R. Soc. London B , vol.348 , pp. 97-105
    • Jaenicke, R.1
  • 5
    • 0027925678 scopus 로고
    • What does protein refolding in vitro tell us about protein folding in the cell?
    • discussion 294-5
    • Jaenicke, R. What does protein refolding in vitro tell us about protein folding in the cell? Philos. Trans. R. Soc. London B. Biol. Sci. 1993, 339, 287-94; discussion 294-5.
    • (1993) Philos. Trans. R. Soc. London B. Biol. Sci. , vol.339 , pp. 287-294
    • Jaenicke, R.1
  • 6
    • 0030251904 scopus 로고    scopus 로고
    • The Specificity of Protein Aggregation
    • Yon, J. M. The Specificity of Protein Aggregation. Nat. Biotechnol. 1996, 14, 1231.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1231
    • Yon, J.M.1
  • 8
    • 0024649936 scopus 로고
    • Heat-induced reversible gelation of arachin: Kinetics, thermodynamics, and protein species involved in the process
    • Kella, N. K. D. Heat-induced reversible gelation of arachin: Kinetics, thermodynamics, and protein species involved in the process. Int. J. Biol. Macromol. 1989, 11, 105-110.
    • (1989) Int. J. Biol. Macromol. , vol.11 , pp. 105-110
    • Kella, N.K.D.1
  • 9
    • 0028567981 scopus 로고
    • A model for the denaturation and aggregation of β-Lactoglobulin
    • Roefs, S. P. F. M.; De Kruif, D. G. A model for the denaturation and aggregation of β-Lactoglobulin. Eur. J. Biochem. 1994, 226, 883-889.
    • (1994) Eur. J. Biochem. , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, D.G.2
  • 10
    • 0028073866 scopus 로고
    • Is stability prediction possible for protein drugs? Denaturation kinetics of β-galactosidase in solution
    • Yoshioka, S.; Aso, Y.; Izutsu, K.; Kojima, S. Is stability prediction possible for protein drugs? Denaturation kinetics of β-galactosidase in solution. Pharm. Res. 1994, 11, 1721-1725.
    • (1994) Pharm. Res. , vol.11 , pp. 1721-1725
    • Yoshioka, S.1    Aso, Y.2    Izutsu, K.3    Kojima, S.4
  • 11
    • 0031573469 scopus 로고    scopus 로고
    • Spectrocopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution
    • Dong, A.; Kendrick, B.; Kreilgard, L.; Matsuura, J.; Manning, M. C.; Carpenter, J. F. Spectrocopic study of secondary structure and thermal denaturation of recombinant human factor XIII in aqueous solution. Arch. Biochem. Biophys. 1997, 347, 213-220.
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 213-220
    • Dong, A.1    Kendrick, B.2    Kreilgard, L.3    Matsuura, J.4    Manning, M.C.5    Carpenter, J.F.6
  • 12
    • 24544447317 scopus 로고
    • Heat-induced gel formation of β-lactoglobulin: A study on the secondary structure and tertiary structure as followed by circular dichroism spectroscopy
    • Matsuura, J.; Manning, M. C. Heat-induced gel formation of β-lactoglobulin: A study on the secondary structure and tertiary structure as followed by circular dichroism spectroscopy. J. Agric. Food Chem. 1994, 42, 1650-1656.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1650-1656
    • Matsuura, J.1    Manning, M.C.2
  • 13
    • 0023664764 scopus 로고
    • Acid unfolding and self-association of recombinant Escherichia coli derived human interferon y
    • Arakawa, T.; Hsu, Y.; Yphantis, D. A. Acid unfolding and self-association of recombinant Escherichia coli derived human interferon y. Biochemistry 1987, 26, 5428-5432.
    • (1987) Biochemistry , vol.26 , pp. 5428-5432
    • Arakawa, T.1    Hsu, Y.2    Yphantis, D.A.3
  • 14
    • 0020435643 scopus 로고
    • Nonspecific stabilization of stress-susceptible proteins by stress- resistant proteins: A model for the biological role of heat shock proteins
    • Minton, K. W.; Karmin, P.; Hahn, G. M.; Minton, A. P. Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins. Proc. Natl. Acad. Sci. U.S.A. 1982, 79, 7107-11.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 7107-7111
    • Minton, K.W.1    Karmin, P.2    Hahn, G.M.3    Minton, A.P.4
  • 15
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • Lumry, R.; Eyring, H. Conformation changes of proteins. J. Phys. Chem. 1954, 58, 110-120.
    • (1954) J. Phys. Chem. , vol.58 , pp. 110-120
    • Lumry, R.1    Eyring, H.2
  • 16
    • 0024318970 scopus 로고
    • pH dependence of the reversible and irreversible thermal denaturation of gamma interferons
    • Mulkerrin, M. G.; Wetzel, R. pH dependence of the reversible and irreversible thermal denaturation of gamma interferons. Biochemistry 1989, 28, 6556-61.
    • (1989) Biochemistry , vol.28 , pp. 6556-6561
    • Mulkerrin, M.G.1    Wetzel, R.2
  • 17
    • 0026734937 scopus 로고
    • Rationalization of the effects of compatible solutes on protein stability in terms of thermodynamic nonideality
    • Winzor, C. L.; Winzor, D. J.; Paleg, L. G.; Jones, G. P.; Naidu, B. P. Rationalization of the effects of compatible solutes on protein stability in terms of thermodynamic nonideality. Arch. Biochem. Biophys. 1992, 296, 102-7.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 102-107
    • Winzor, C.L.1    Winzor, D.J.2    Paleg, L.G.3    Jones, G.P.4    Naidu, B.P.5
  • 18
    • 0022370032 scopus 로고
    • Preparation and characterization of recombinant DNA-derived human interferon-gamma
    • Arakawa, T.; Alton, N. K.; Hsu, Y. R. Preparation and characterization of recombinant DNA-derived human interferon-gamma. J. Biol. Chem. 1985, 260, 14435-9.
    • (1985) J. Biol. Chem. , vol.260 , pp. 14435-14439
    • Arakawa, T.1    Alton, N.K.2    Hsu, Y.R.3
  • 20
    • 0022333536 scopus 로고
    • Structural studies on acid unfolding and refolding of recombinant human interferon gamma
    • Hsu, Y. R.; Arakawa, T. Structural studies on acid unfolding and refolding of recombinant human interferon gamma. Biochemistry 1985, 24, 7959-63.
    • (1985) Biochemistry , vol.24 , pp. 7959-7963
    • Hsu, Y.R.1    Arakawa, T.2
  • 21
    • 0023664830 scopus 로고
    • Sedimentation equilibrium measurements of recombinant DNA derived human interferon gamma
    • Yphantis, D. A.; Arakawa, T. Sedimentation equilibrium measurements of recombinant DNA derived human interferon gamma. Biochemistry 1987, 26, 5422-7.
    • (1987) Biochemistry , vol.26 , pp. 5422-5427
    • Yphantis, D.A.1    Arakawa, T.2
  • 22
    • 0029786225 scopus 로고    scopus 로고
    • Production, purification, and characterization of a highly glucose- Tolerant novel beta-glucosidase from Candida peltata
    • Saha, B. C.; Bothast, R. J. Production, purification, and characterization of a highly glucose-tolerant novel beta-glucosidase from Candida peltata. Appl. Environ. Microbiol. 1996, 62, 3165-70.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3165-3170
    • Saha, B.C.1    Bothast, R.J.2
  • 24
    • 0024419094 scopus 로고
    • Hydrophobic interaction chromatography in alkaline pH
    • Narhi, L. O.; Kita, Y.; Arakawa, T. Hydrophobic interaction chromatography in alkaline pH. Anal. Biochem. 1989, 182, 266-70.
    • (1989) Anal. Biochem. , vol.182 , pp. 266-270
    • Narhi, L.O.1    Kita, Y.2    Arakawa, T.3
  • 25
    • 0023068339 scopus 로고
    • Salting-out adsorption techniques for protein purification
    • Porath, J. Salting-out adsorption techniques for protein purification. Biopolymers 1987, 26 Suppl, S193-204.
    • (1987) Biopolymers , vol.26 , Issue.SUPPL.
    • Porath, J.1
  • 26
    • 0027310845 scopus 로고
    • The control of protein stability and association by weak interactions with water: How do solvents affect these processes?
    • Timasheff, S. N. The control of protein stability and association by weak interactions with water: How do solvents affect these processes? Annu. Rev. Biophys. Biomol. Struct. 1993, 22, 67-97.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 67-97
    • Timasheff, S.N.1
  • 27
    • 0024506309 scopus 로고
    • Structure-function relationships in the inorganic salt-induced precipitation of alpha-chymotrypsin
    • Przybycien, T. M.; Bailey, J. E. Structure-function relationships in the inorganic salt-induced precipitation of alpha-chymotrypsin. Biochim. Biophys. Acta 1989, 995, 231-45.
    • (1989) Biochim. Biophys. Acta , vol.995 , pp. 231-245
    • Przybycien, T.M.1    Bailey, J.E.2
  • 28
    • 0030824333 scopus 로고    scopus 로고
    • Drug delivery matrix containing native protein precipitates suspended in a poloxamer gel
    • Stratton, L. P.; Dong, A.; Manning, M. C.; Carpenter, J. F. Drug delivery matrix containing native protein precipitates suspended in a poloxamer gel. J. Pharm. Sci. 1997, 86, 1006-1010.
    • (1997) J. Pharm. Sci. , vol.86 , pp. 1006-1010
    • Stratton, L.P.1    Dong, A.2    Manning, M.C.3    Carpenter, J.F.4
  • 29
    • 85030349722 scopus 로고    scopus 로고
    • Protein Solutions, Inc. Charlottesville, VA 22901
    • Protein Solutions, I. DynaPro-801WIN Operators Manual. Protein Solutions, Inc. Charlottesville, VA 22901, 1997.
    • (1997) DynaPro-801WIN Operators Manual
  • 30
    • 0030041320 scopus 로고    scopus 로고
    • Infrared and circular dichroism spectroscopic characterization of structural differences between beta-lactoglobulin A and B
    • Dong, A.; Matsuura, J.; Allison, S. D.; Chrisman, E.; Manning, M. C.; Carpenter, J. F. Infrared and circular dichroism spectroscopic characterization of structural differences between beta-lactoglobulin A and B. Biochemistry 1996, 35, 1450-7.
    • (1996) Biochemistry , vol.35 , pp. 1450-1457
    • Dong, A.1    Matsuura, J.2    Allison, S.D.3    Chrisman, E.4    Manning, M.C.5    Carpenter, J.F.6
  • 31
    • 0028307232 scopus 로고
    • Infrared methods for study of hemoglobin reactions and structures
    • Dong, A.; Caughey, W. S. Infrared methods for study of hemoglobin reactions and structures. Methods Enzymol. 1994, 232, 139-75.
    • (1994) Methods Enzymol. , vol.232 , pp. 139-175
    • Dong, A.1    Caughey, W.S.2
  • 32
    • 0030059491 scopus 로고    scopus 로고
    • Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states
    • Kendrick, B. S.; Dong, A.; Allison, S. D.; Manning, M. C.; Carpenter, J. F. Quantitation of the area of overlap between second-derivative amide I infrared spectra to determine the structural similarity of a protein in different states. J. Pharm. Sci. 1996, 85, 155-158.
    • (1996) J. Pharm. Sci. , vol.85 , pp. 155-158
    • Kendrick, B.S.1    Dong, A.2    Allison, S.D.3    Manning, M.C.4    Carpenter, J.F.5
  • 33
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T.; Wu, C. C.; Martinez, H. M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 1986, 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.C.2    Martinez, H.M.3
  • 34
    • 0024281290 scopus 로고
    • Differential scanning calorimetry of the irreversible thermal denaturation of thermolysm
    • Sanchez-Ruiz, J. M.; Lopez-Lacomba, J. L.; Cortijo, M.; Mateo, P. L. Differential scanning calorimetry of the irreversible thermal denaturation of thermolysm. Biochemistry 1988, 27, 1648-1652.
    • (1988) Biochemistry , vol.27 , pp. 1648-1652
    • Sanchez-Ruiz, J.M.1    Lopez-Lacomba, J.L.2    Cortijo, M.3    Mateo, P.L.4
  • 35
    • 0000057219 scopus 로고
    • The effect of light scattering on ultraviolet difference spectra
    • Leach, S. J.; Scheraga, H. A. The effect of light scattering on ultraviolet difference spectra. J. Am. Chem. Soc. 1960, 82, 4790-4792.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 4790-4792
    • Leach, S.J.1    Scheraga, H.A.2
  • 36
    • 0025357111 scopus 로고
    • Protein secondary structures in water from second-derivative amide I infrared spectra
    • Dong, A.; Huang, P.; Caughey, W. S. Protein secondary structures in water from second-derivative amide I infrared spectra. Biochemistry 1990, 29, 3303-8.
    • (1990) Biochemistry , vol.29 , pp. 3303-3308
    • Dong, A.1    Huang, P.2    Caughey, W.S.3
  • 37
    • 0022463740 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • Susi, H.; Byler, D. M. Resolution-enhanced Fourier transform infrared spectroscopy of enzymes. Methods Enzymol. 1986, 130, 290-311.
    • (1986) Methods Enzymol. , vol.130 , pp. 290-311
    • Susi, H.1    Byler, D.M.2
  • 38
    • 0026613095 scopus 로고
    • 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma
    • Grzesiek, S.; Dobeli, H.; Gentz, R.; Garotta, G.; Labhardt, A. M.; Bax, A. 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma. Biochemistry 1992, 31, 8180-90.
    • (1992) Biochemistry , vol.31 , pp. 8180-8190
    • Grzesiek, S.1    Dobeli, H.2    Gentz, R.3    Garotta, G.4    Labhardt, A.M.5    Bax, A.6
  • 39
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler, D. M.; Susi, H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 1986, 25, 469-487.
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 40
    • 0015950174 scopus 로고
    • Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride
    • Lee, J. C.; Timasheff, S. N. Partial specific volumes and interactions with solvent components of proteins in guanidine hydrochloride. Biochemistry 1974, 13, 257-65.
    • (1974) Biochemistry , vol.13 , pp. 257-265
    • Lee, J.C.1    Timasheff, S.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.