메뉴 건너뛰기




Volumn 6, Issue 5, 2011, Pages

Urate oxidase purification by salting-in crystallization: Towards an alternative to chromatography

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIUM CHLORIDE; MACROGOL; POLYMER; RASBURICASE; URATE OXIDASE; INORGANIC SALT;

EID: 79955888189     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0019013     Document Type: Article
Times cited : (15)

References (39)
  • 1
    • 0029395001 scopus 로고
    • Protein purification by bulk crystallization: the recovery of ovalbumin
    • Judge RA, Johns MR, White ET, (1995) Protein purification by bulk crystallization: the recovery of ovalbumin. Biotechnol Bioeng 48: 316-323.
    • (1995) Biotechnol Bioeng , vol.48 , pp. 316-323
    • Judge, R.A.1    Johns, M.R.2    White, E.T.3
  • 2
    • 0032549475 scopus 로고    scopus 로고
    • Nucleation and growth of microbial lipase crystals from clarified concentrated fermentation broths
    • Jacobsen C, Garside J, Hoare M, (1998) Nucleation and growth of microbial lipase crystals from clarified concentrated fermentation broths. Biotechnology and Bioengineering 57: 666-675.
    • (1998) Biotechnology and Bioengineering , vol.57 , pp. 666-675
    • Jacobsen, C.1    Garside, J.2    Hoare, M.3
  • 3
    • 0026592267 scopus 로고
    • Two independent mutational events in the loss of urate oxidase during hominoid evolution
    • Wu XW, Muzny DM, Lee CC, Caskey CT, (1992) Two independent mutational events in the loss of urate oxidase during hominoid evolution. J Mol Evol 34: 78-84.
    • (1992) J Mol Evol , vol.34 , pp. 78-84
    • Wu, X.W.1    Muzny, D.M.2    Lee, C.C.3    Caskey, C.T.4
  • 4
    • 0019787519 scopus 로고
    • Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis
    • Ames BN, Cathcart R, Schwiers E, Hochstein P, (1981) Uric acid provides an antioxidant defense in humans against oxidant- and radical-caused aging and cancer: a hypothesis. Proc Natl Acad Sci 78: 6858-6862.
    • (1981) Proc Natl Acad Sci , vol.78 , pp. 6858-6862
    • Ames, B.N.1    Cathcart, R.2    Schwiers, E.3    Hochstein, P.4
  • 5
    • 85179206019 scopus 로고    scopus 로고
    • Directory of Therapeutic Enzymes
    • In: McGrath B, Walsh G, editors, CRC Press
    • McGrath B, Walsh G, (2005) Directory of Therapeutic Enzymes. In: McGrath B, Walsh G, editors. CRC Press.
    • (2005)
    • McGrath, B.1    Walsh, G.2
  • 6
    • 0036347379 scopus 로고    scopus 로고
    • Modification of a reactive cysteine explains differences between rasburicase end uricozyme, a natural Aspergillus flavus uricase
    • Bayol A, Capdevielle J, Malazzi P, Buzy A, Bonnet MC, et al. (2002) Modification of a reactive cysteine explains differences between rasburicase end uricozyme, a natural Aspergillus flavus uricase. Biotechnol Appl Biochem 36: 21-31.
    • (2002) Biotechnol Appl Biochem , vol.36 , pp. 21-31
    • Bayol, A.1    Capdevielle, J.2    Malazzi, P.3    Buzy, A.4    Bonnet, M.C.5
  • 7
    • 33947257299 scopus 로고    scopus 로고
    • Rasburicase represents a new tool for hyperuricemia in tumor lysis syndrome and in gout
    • Cammalleri L, Malaguarnera M, (2007) Rasburicase represents a new tool for hyperuricemia in tumor lysis syndrome and in gout. Int J Med Sci 4: 83-93.
    • (2007) Int J Med Sci , vol.4 , pp. 83-93
    • Cammalleri, L.1    Malaguarnera, M.2
  • 9
  • 10
    • 0002889635 scopus 로고
    • Direct crystallization of lysozyme from egg white and some crystalline salts of lysozyme
    • Alderton G, Fevold H, (1946) Direct crystallization of lysozyme from egg white and some crystalline salts of lysozyme. J Biological Chemistry 146: 1-5.
    • (1946) J Biological Chemistry , vol.146 , pp. 1-5
    • Alderton, G.1    Fevold, H.2
  • 13
    • 0015493834 scopus 로고
    • Purification and characterisation of crystalline -amylase from barley
    • Visuri K, Nummi M, (1972) Purification and characterisation of crystalline-amylase from barley. Eur J Biochem 28: 555-565.
    • (1972) Eur J Biochem , vol.28 , pp. 555-565
    • Visuri, K.1    Nummi, M.2
  • 17
    • 39749179770 scopus 로고    scopus 로고
    • Crystallization as a purification method for Jack Bean Urease: on the suitability of Poly(Ethylene Glycol), Li2SO4, and NaCl as precipitants
    • Weber M, Jones M, Ulrich J, (2008) Crystallization as a purification method for Jack Bean Urease: on the suitability of Poly(Ethylene Glycol), Li2SO4, and NaCl as precipitants. Crystal Growth and Design 8: 711-716.
    • (2008) Crystal Growth and Design , vol.8 , pp. 711-716
    • Weber, M.1    Jones, M.2    Ulrich, J.3
  • 18
    • 0001470914 scopus 로고
    • The isolation and crystallization of the enzyme urease
    • Sumner J, (1926) The isolation and crystallization of the enzyme urease. Journal of Biological Chemistry 69: 435-441.
    • (1926) Journal of Biological Chemistry , vol.69 , pp. 435-441
    • Sumner, J.1
  • 19
    • 2642558909 scopus 로고    scopus 로고
    • Liquid-liquid phase separations in urate oxidase/PEG mixtures: characterization and implications for protein crystallization
    • Vivares D, Bonneté F, (2004) Liquid-liquid phase separations in urate oxidase/PEG mixtures: characterization and implications for protein crystallization. J Phys Chem B 108: 6498.
    • (2004) J Phys Chem B , vol.108 , pp. 6498
    • Vivares, D.1    Bonneté, F.2
  • 23
    • 0035502143 scopus 로고    scopus 로고
    • Interactions in solution and crystallization of Aspergillus flavus urate oxidase
    • Bonneté F, Vivares D, Robert C, Colloc'h N, (2001) Interactions in solution and crystallization of Aspergillus flavus urate oxidase. J Crystal Growth 232: 330-339.
    • (2001) J Crystal Growth , vol.232 , pp. 330-339
    • Bonneté, F.1    Vivares, D.2    Robert, C.3    Colloc'h, N.4
  • 24
    • 0036006284 scopus 로고    scopus 로고
    • X-ray scattering studies of Aspergillus flavus urate oxidase: towards a better understanding of PEG effects on the crystallization of large proteins
    • Vivares D, Bonneté F, (2002) X-ray scattering studies of Aspergillus flavus urate oxidase: towards a better understanding of PEG effects on the crystallization of large proteins. Acta Cryst D58: 472-479.
    • (2002) Acta Cryst , vol.D58 , pp. 472-479
    • Vivares, D.1    Bonneté, F.2
  • 25
    • 0036769001 scopus 로고    scopus 로고
    • Catching the PEG-induced attractive interaction between proteins
    • Vivares D, Belloni L, Tardieu A, Bonneté F, (2002) Catching the PEG-induced attractive interaction between proteins. Eur Phys J E 9: 15-25.
    • (2002) Eur Phys J E , vol.9 , pp. 15-25
    • Vivares, D.1    Belloni, L.2    Tardieu, A.3    Bonneté, F.4
  • 26
    • 0033513785 scopus 로고    scopus 로고
    • Second virial coefficient: variations with lysozyme crystallization conditions
    • Bonneté F, Finet S, Tardieu A, (1999) Second virial coefficient: variations with lysozyme crystallization conditions. J Crystal Growth 196: 403-414.
    • (1999) J Crystal Growth , vol.196 , pp. 403-414
    • Bonneté, F.1    Finet, S.2    Tardieu, A.3
  • 28
    • 0033513794 scopus 로고    scopus 로고
    • Proteins in solution: from X-ray scattering intensities to interaction potentials
    • Tardieu A, Le Verge A, Riès-Kautt M, Malfois M, Bonneté F, et al. (1999) Proteins in solution: from X-ray scattering intensities to interaction potentials. J Crystal Growth 196: 193-203.
    • (1999) J Crystal Growth , vol.196 , pp. 193-203
    • Tardieu, A.1    Le Verge, A.2    Riès-Kautt, M.3    Malfois, M.4    Bonneté, F.5
  • 29
    • 0000478452 scopus 로고    scopus 로고
    • A model of attractive interactions to account for fluid-fluid phase separation of protein solutions
    • Malfois M, Bonnete F, Belloni L, Tardieu A, (1996) A model of attractive interactions to account for fluid-fluid phase separation of protein solutions. The Journal of Chemical Physics 105: 3290-3300.
    • (1996) The Journal of Chemical Physics , vol.105 , pp. 3290-3300
    • Malfois, M.1    Bonnete, F.2    Belloni, L.3    Tardieu, A.4
  • 32
    • 0037109740 scopus 로고    scopus 로고
    • A colorimetric 96-well microtiter plate assay for the determination of urate oxidase activity and its kinetic parameters
    • Fraisse L, Bonnet MC, De Farcy JP, Agut C, Dersigny D, et al. (2002) A colorimetric 96-well microtiter plate assay for the determination of urate oxidase activity and its kinetic parameters. Anal Biochem 309: 173-179.
    • (2002) Anal Biochem , vol.309 , pp. 173-179
    • Fraisse, L.1    Bonnet, M.C.2    De Farcy, J.P.3    Agut, C.4    Dersigny, D.5
  • 35
    • 0028802747 scopus 로고
    • Relative effectiveness of various anions on the solubility of acidic Hypoderma lineatum collagenase at pH 7.2
    • Carbonnaux C, Riès-Kautt M, Ducruix A, (1995) Relative effectiveness of various anions on the solubility of acidic Hypoderma lineatum collagenase at pH 7.2. Protein Sci 4: 2123-2128.
    • (1995) Protein Sci , vol.4 , pp. 2123-2128
    • Carbonnaux, C.1    Riès-Kautt, M.2    Ducruix, A.3
  • 36
    • 0024969402 scopus 로고
    • Relative effectiveness of various ions on the solubility and crystal growth of lysozyme
    • Riès-Kautt M, Ducruix A, (1989) Relative effectiveness of various ions on the solubility and crystal growth of lysozyme. J Biol Chem 264: 745-748.
    • (1989) J Biol Chem , vol.264 , pp. 745-748
    • Riès-Kautt, M.1    Ducruix, A.2
  • 37
    • 0032311408 scopus 로고    scopus 로고
    • Improved isolation and crystallization of photosystem I for structural analysis
    • Fromme P, Witt HT, (1998) Improved isolation and crystallization of photosystem I for structural analysis. Biochimica et Biophysica Acta (BBA)- Bioenergetics 1365: 175-184.
    • (1998) Biochimica Et Biophysica Acta (BBA) - Bioenergetics , vol.1365 , pp. 175-184
    • Fromme, P.1    Witt, H.T.2
  • 38
    • 0342813099 scopus 로고    scopus 로고
    • No salting-in of lysozyme chloride observed at low ionic strength over a large range of pH
    • Retailleau P, Ries-Kautt M, Ducruix A, (1997) No salting-in of lysozyme chloride observed at low ionic strength over a large range of pH. Biophys J 73: 2156-2163.
    • (1997) Biophys J , vol.73 , pp. 2156-2163
    • Retailleau, P.1    Ries-Kautt, M.2    Ducruix, A.3
  • 39
    • 0344234380 scopus 로고    scopus 로고
    • Controlling biomolecular crystallization by understanding the distinct effects of PEGs and salts on solubility
    • Finet S, Vivarès D, Bonneté F, Tardieu A, (2003) Controlling biomolecular crystallization by understanding the distinct effects of PEGs and salts on solubility. Methods in Enzymology. 368: 105-129.
    • (2003) Methods in Enzymology , vol.368 , pp. 105-129
    • Finet, S.1    Vivarès, D.2    Bonneté, F.3    Tardieu, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.