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Volumn 86, Issue 1, 2008, Pages 43-52

Optimisation of isolation and purification of the jack bean enzyme urease by extraction and subsequent crystallization

Author keywords

Down stream processing; Extraction; Jack bean urease; Protein crystallization; Protein purification

Indexed keywords

CRYSTALLIZATION; EXTRACTION; OPTIMIZATION; PROTEINS; PURIFICATION;

EID: 41849116376     PISSN: 09603085     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fbp.2007.10.005     Document Type: Article
Times cited : (26)

References (51)
  • 1
    • 0036794621 scopus 로고    scopus 로고
    • Strong and specific effects of cations on lysozyme chloride solubility
    • Benas P., Legrand L., and Riés-Kautt M. Strong and specific effects of cations on lysozyme chloride solubility. Acta Crystallogr D 58 (2002) 1582-1587
    • (2002) Acta Crystallogr D , vol.58 , pp. 1582-1587
    • Benas, P.1    Legrand, L.2    Riés-Kautt, M.3
  • 2
    • 0347308440 scopus 로고    scopus 로고
    • Measurement and modelling of protein crystal nucleation kinetics
    • Bhamidi V., Varanasi S., and Schall C.A. Measurement and modelling of protein crystal nucleation kinetics. Cryst Growth Des 2 (2002) 395-400
    • (2002) Cryst Growth Des , vol.2 , pp. 395-400
    • Bhamidi, V.1    Varanasi, S.2    Schall, C.A.3
  • 3
    • 0014514830 scopus 로고
    • Jack bean urease (EC 3.5.1.5). A new purification and reliable rate assay
    • Blakeley R.L., Webb E.C., and Zerner B. Jack bean urease (EC 3.5.1.5). A new purification and reliable rate assay. Biochemistry-US 8 (1969) 1984-1990
    • (1969) Biochemistry-US , vol.8 , pp. 1984-1990
    • Blakeley, R.L.1    Webb, E.C.2    Zerner, B.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0042982349 scopus 로고    scopus 로고
    • Quantifying main trends in lysozyme nucleation: the effect of precipitant concentration, supersaturation, and impurities
    • Burke M.W., Leardi R., Judge R.A., and Pusey M.L. Quantifying main trends in lysozyme nucleation: the effect of precipitant concentration, supersaturation, and impurities. Cryst Growth Des 1 (2001) 333-337
    • (2001) Cryst Growth Des , vol.1 , pp. 333-337
    • Burke, M.W.1    Leardi, R.2    Judge, R.A.3    Pusey, M.L.4
  • 6
    • 0024036036 scopus 로고
    • Solubility of glucose isomerase in ammonium sulfate solutions
    • Chayen N., Akins J., Campbell-Smith S., and Blow D.M. Solubility of glucose isomerase in ammonium sulfate solutions. J Cryst Growth 90 (1988) 112-116
    • (1988) J Cryst Growth , vol.90 , pp. 112-116
    • Chayen, N.1    Akins, J.2    Campbell-Smith, S.3    Blow, D.M.4
  • 7
    • 0013515383 scopus 로고
    • An improved method for recrystallizing urease
    • Dounce A.L. An improved method for recrystallizing urease. J Biol Chem 140 (1941) 307-308
    • (1941) J Biol Chem , vol.140 , pp. 307-308
    • Dounce, A.L.1
  • 8
    • 0003492872 scopus 로고    scopus 로고
    • Methods of crystallization
    • Ducruix A., and Giegé R. (Eds), Oxford University Press, Oxford, UK
    • Ducruix A., and Giegé R. Methods of crystallization. In: Ducruix A., and Giegé R. (Eds). Crystallization of Nucleic Acids and Proteins (2000), Oxford University Press, Oxford, UK 121-148
    • (2000) Crystallization of Nucleic Acids and Proteins , pp. 121-148
    • Ducruix, A.1    Giegé, R.2
  • 9
    • 0035890872 scopus 로고    scopus 로고
    • Canatoxin, a toxic protein from jack beans (Canavalia ensiformis), is a variant form of urease (EC 3.5.1.5): biological effects of urease independent of its ureolytic activity
    • Follmer C., Barcellos G.B.S., Zingali R.B., Machado O.L.T., Alves E.W., Barja-Fidalgo C., Guimaraes J.A., and Carlini C.R. Canatoxin, a toxic protein from jack beans (Canavalia ensiformis), is a variant form of urease (EC 3.5.1.5): biological effects of urease independent of its ureolytic activity. Biochem J 360 (2001) 217-224
    • (2001) Biochem J , vol.360 , pp. 217-224
    • Follmer, C.1    Barcellos, G.B.S.2    Zingali, R.B.3    Machado, O.L.T.4    Alves, E.W.5    Barja-Fidalgo, C.6    Guimaraes, J.A.7    Carlini, C.R.8
  • 10
    • 0032677214 scopus 로고    scopus 로고
    • Tetragonal chicken egg white lysozyme solubility in sodium chloride solutions
    • Forsythe E.L., Judge R.A., and Pusey M.L. Tetragonal chicken egg white lysozyme solubility in sodium chloride solutions. J Chem Eng Data 44 (1999) 637-640
    • (1999) J Chem Eng Data , vol.44 , pp. 637-640
    • Forsythe, E.L.1    Judge, R.A.2    Pusey, M.L.3
  • 11
    • 0035502089 scopus 로고    scopus 로고
    • Nucleation of protein crystals: critical nuclei, phase behaviour, and control pathways
    • Galkin O., and Vekilov P.G. Nucleation of protein crystals: critical nuclei, phase behaviour, and control pathways. J Cryst Growth 232 (2001) 63-76
    • (2001) J Cryst Growth , vol.232 , pp. 63-76
    • Galkin, O.1    Vekilov, P.G.2
  • 12
    • 0013957591 scopus 로고
    • A new method of assay and the specific enzymic activity
    • Gorin G., and Chin C.-C. A new method of assay and the specific enzymic activity. Anal Biochem 17 (1966) 49-59
    • (1966) Anal Biochem , vol.17 , pp. 49-59
    • Gorin, G.1    Chin, C.-C.2
  • 13
    • 16444383384 scopus 로고    scopus 로고
    • Effects of kinetic roughening and liquid-liquid phase transition on lysozyme crystal growth velocities
    • Gorti S., Konnert J., Forsythe E.L., and Pusey M.L. Effects of kinetic roughening and liquid-liquid phase transition on lysozyme crystal growth velocities. Cryst Growth Des 5 (2005) 535-545
    • (2005) Cryst Growth Des , vol.5 , pp. 535-545
    • Gorti, S.1    Konnert, J.2    Forsythe, E.L.3    Pusey, M.L.4
  • 15
    • 36949094073 scopus 로고
    • High-yield crystallization of urease from jack bean
    • Hanabusa K. High-yield crystallization of urease from jack bean. Nature 189 (1961) 551-553
    • (1961) Nature , vol.189 , pp. 551-553
    • Hanabusa, K.1
  • 16
    • 0001916518 scopus 로고    scopus 로고
    • Urease
    • Messerschmidt A., Huber R., Poulos T., and Wieghardt K. (Eds), John Wiley & Sons, New York, USA
    • Hausinger R.P., and Karplus A. Urease. In: Messerschmidt A., Huber R., Poulos T., and Wieghardt K. (Eds). Handbook of Metalloproteins vol. 2 (2001), John Wiley & Sons, New York, USA 867-879
    • (2001) Handbook of Metalloproteins , vol.2 , pp. 867-879
    • Hausinger, R.P.1    Karplus, A.2
  • 17
    • 0028845991 scopus 로고
    • Crystal-structure of concanavalin B at 1.65 angstrom resolution-an inactivated chitinase from seeds of Canavalia ensiformis
    • Hennig M., Jansonius J.N., Vanscheltinga A.C.T., Dijkstra B.W., and Schlesier B. Crystal-structure of concanavalin B at 1.65 angstrom resolution-an inactivated chitinase from seeds of Canavalia ensiformis. J Mol Biol 254 2 (1995) 237-246
    • (1995) J Mol Biol , vol.254 , Issue.2 , pp. 237-246
    • Hennig, M.1    Jansonius, J.N.2    Vanscheltinga, A.C.T.3    Dijkstra, B.W.4    Schlesier, B.5
  • 19
    • 0026803290 scopus 로고
    • Preliminary crystallographic studies of urease from jack bean and from Klebsiella aerogenes
    • Jabri E., Lee M.H., Hausinger R.P., and Karplus P.A. Preliminary crystallographic studies of urease from jack bean and from Klebsiella aerogenes. J Mol Biol 227 (1992) 934-937
    • (1992) J Mol Biol , vol.227 , pp. 934-937
    • Jabri, E.1    Lee, M.H.2    Hausinger, R.P.3    Karplus, P.A.4
  • 20
    • 27344444155 scopus 로고
    • Some proteins from the jack bean, Canavalia ensiformis
    • Jones D.B., and Johns O.C. Some proteins from the jack bean, Canavalia ensiformis. J Biol Chem 28 (1916) 67-75
    • (1916) J Biol Chem , vol.28 , pp. 67-75
    • Jones, D.B.1    Johns, O.C.2
  • 21
    • 29444435253 scopus 로고    scopus 로고
    • Industrial crystallization of proteins-a question of activity
    • Jones M.J., and Ulrich J. Industrial crystallization of proteins-a question of activity. Chemie Ingenieur Technik 77 (2005) 1527-1533
    • (2005) Chemie Ingenieur Technik , vol.77 , pp. 1527-1533
    • Jones, M.J.1    Ulrich, J.2
  • 22
    • 0029395001 scopus 로고
    • Protein purification by bulk crystallization: the recovery of ovalbumin
    • Judge R.A., Johns M.R., and White E.T. Protein purification by bulk crystallization: the recovery of ovalbumin. Biotechnol Bioeng 48 (1995) 316-323
    • (1995) Biotechnol Bioeng , vol.48 , pp. 316-323
    • Judge, R.A.1    Johns, M.R.2    White, E.T.3
  • 23
    • 0030134315 scopus 로고    scopus 로고
    • Solubility of ovalbumin in ammonium sulfate solutions
    • Judge R.A., Johns M.R., and White E.T. Solubility of ovalbumin in ammonium sulfate solutions. J Chem Eng Data 412 (1996) 422-424
    • (1996) J Chem Eng Data , vol.412 , pp. 422-424
    • Judge, R.A.1    Johns, M.R.2    White, E.T.3
  • 24
    • 0033567233 scopus 로고    scopus 로고
    • The N-glycans of jack bean α-mannosidase. Structure, topology and function
    • Kimura Y., Hess D., and Sturm A. The N-glycans of jack bean α-mannosidase. Structure, topology and function. Eur J Biochem 264 (1999) 168-175
    • (1999) Eur J Biochem , vol.264 , pp. 168-175
    • Kimura, Y.1    Hess, D.2    Sturm, A.3
  • 25
    • 0003952619 scopus 로고    scopus 로고
    • Biochemical aspects and handling of macromolecular solutions
    • Ducruix A., and Giegé R. (Eds), Oxford University Press, Oxford, UK
    • Lorber B., and Giegé R. Biochemical aspects and handling of macromolecular solutions. In: Ducruix A., and Giegé R. (Eds). Crystallization of Nucleic Acids and Proteins (2000), Oxford University Press, Oxford, UK 17-44
    • (2000) Crystallization of Nucleic Acids and Proteins , pp. 17-44
    • Lorber, B.1    Giegé, R.2
  • 26
    • 0014201066 scopus 로고
    • Some properties and purifications of urease
    • Lynn K.R. Some properties and purifications of urease. Biochim Biophys Acta 146 (1967) 205-218
    • (1967) Biochim Biophys Acta , vol.146 , pp. 205-218
    • Lynn, K.R.1
  • 27
    • 0013853290 scopus 로고
    • Urease. V. Some observations on the procedure for its isolation
    • Mamiya G., and Gorin G. Urease. V. Some observations on the procedure for its isolation. Biochim Biophys Acta 105 (1965) 382-385
    • (1965) Biochim Biophys Acta , vol.105 , pp. 382-385
    • Mamiya, G.1    Gorin, G.2
  • 28
    • 0014181667 scopus 로고
    • The association and dissociation of concanavalin A, the phytohemagglutinin of the jack bean
    • Olson M.O., and Liener I.E. The association and dissociation of concanavalin A, the phytohemagglutinin of the jack bean. Biochemistry 6 12 (1967) 3801-3808
    • (1967) Biochemistry , vol.6 , Issue.12 , pp. 3801-3808
    • Olson, M.O.1    Liener, I.E.2
  • 29
    • 0036793453 scopus 로고    scopus 로고
    • Importance of the nature of anions in lysozyme crystallization correlated with protein net charge variation
    • Retailleau P., Ducruix A., and Riés-Kautt M. Importance of the nature of anions in lysozyme crystallization correlated with protein net charge variation. Acta Crystallogr D 58 (2002) 1576-1581
    • (2002) Acta Crystallogr D , vol.58 , pp. 1576-1581
    • Retailleau, P.1    Ducruix, A.2    Riés-Kautt, M.3
  • 30
    • 0030566049 scopus 로고    scopus 로고
    • Nucleation and crystallization of globular proteins-what we know and what is missing
    • Rosenberger F., Vekilov R.G., Muschol M., and Thomas B.R. Nucleation and crystallization of globular proteins-what we know and what is missing. J Cryst Growth 168 (1996) 1-27
    • (1996) J Cryst Growth , vol.168 , pp. 1-27
    • Rosenberger, F.1    Vekilov, R.G.2    Muschol, M.3    Thomas, B.R.4
  • 31
    • 41849140750 scopus 로고    scopus 로고
    • X-ray analysis
    • Ducruix A., and Giegé R. (Eds), Oxford University Press, Oxford, UK
    • Sawyer L., and Turner M.A. X-ray analysis. In: Ducruix A., and Giegé R. (Eds). Crystallization of Nucleic Acids and Proteins (2000), Oxford University Press, Oxford, UK 391-420
    • (2000) Crystallization of Nucleic Acids and Proteins , pp. 391-420
    • Sawyer, L.1    Turner, M.A.2
  • 32
    • 0008145354 scopus 로고    scopus 로고
    • Characterization of a class II chitinase from jack bean (Canavalia ensiformis) seeds (Short communication)
    • Schlesier B., Koch G., and Horstmann C. Characterization of a class II chitinase from jack bean (Canavalia ensiformis) seeds (Short communication). Nahrung 42 3-4 (1998) 170
    • (1998) Nahrung , vol.42 , Issue.3-4 , pp. 170
    • Schlesier, B.1    Koch, G.2    Horstmann, C.3
  • 33
    • 0032520174 scopus 로고    scopus 로고
    • Purification and characterization of N-glycanase, a concanavalin A binding protein from jackbean (Canavalia Ensiformis)
    • Sheldon P.S., Keen J.N., and Bowles D.J. Purification and characterization of N-glycanase, a concanavalin A binding protein from jackbean (Canavalia Ensiformis). Biochem J 330 (1998) 13-20
    • (1998) Biochem J , vol.330 , pp. 13-20
    • Sheldon, P.S.1    Keen, J.N.2    Bowles, D.J.3
  • 34
    • 0036008537 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray structure determination of jack bean urease with a bound antibody fragment
    • Sheridan L., Wilmot C.M., Cromie K.D., van der Logt P., and Phillips S.E.V. Crystallization and preliminary X-ray structure determination of jack bean urease with a bound antibody fragment. Acta Crystallogr D 58 (2002) 374-376
    • (2002) Acta Crystallogr D , vol.58 , pp. 374-376
    • Sheridan, L.1    Wilmot, C.M.2    Cromie, K.D.3    van der Logt, P.4    Phillips, S.E.V.5
  • 35
    • 0000521374 scopus 로고
    • Biochemical characterization of canavalin, the major storage protein of jack bean
    • Smith S.C., Johnson S., Andrews J., and McPherson A. Biochemical characterization of canavalin, the major storage protein of jack bean. Plant Physiol 70 (1982) 1199-1209
    • (1982) Plant Physiol , vol.70 , pp. 1199-1209
    • Smith, S.C.1    Johnson, S.2    Andrews, J.3    McPherson, A.4
  • 36
    • 0000124774 scopus 로고
    • The globulins of the jack bean, Canavalia ensiformis
    • Sumner J.B. The globulins of the jack bean, Canavalia ensiformis. J Biol Chem 37 (1919) 137-141
    • (1919) J Biol Chem , vol.37 , pp. 137-141
    • Sumner, J.B.1
  • 37
    • 0001470914 scopus 로고
    • The isolation and crystallization of the enzyme urease
    • Sumner J.B. The isolation and crystallization of the enzyme urease. J Biol Chem 69 (1926) 435-441
    • (1926) J Biol Chem , vol.69 , pp. 435-441
    • Sumner, J.B.1
  • 38
    • 0010067749 scopus 로고
    • Note. The recrystallization of urease
    • Sumner J.B. Note. The recrystallization of urease. J Biol Chem 70 (1926) 97-98
    • (1926) J Biol Chem , vol.70 , pp. 97-98
    • Sumner, J.B.1
  • 39
    • 0000997583 scopus 로고
    • Urease
    • Sumner J.B., and Myrbäck K. (Eds), Academic Press, New York, USA
    • Sumner J.B. Urease. In: Sumner J.B., and Myrbäck K. (Eds). The Enzymes. Chemistry and Mechanism of Action vol. 1, part 2 (1951), Academic Press, New York, USA 873-892
    • (1951) The Enzymes. Chemistry and Mechanism of Action , vol.1 PART 2 , pp. 873-892
    • Sumner, J.B.1
  • 40
    • 10544238258 scopus 로고
    • Crystalline urease II
    • Sumner J.B., and Hand D.B. Crystalline urease II. J Biol Chem 76 (1928) 149-162
    • (1928) J Biol Chem , vol.76 , pp. 149-162
    • Sumner, J.B.1    Hand, D.B.2
  • 41
    • 33947352794 scopus 로고
    • The isoelectric point of crystalline urease
    • Sumner J.B., and Hand D.B. The isoelectric point of crystalline urease. J Am Chem Soc 51 (1929) 1255-1260
    • (1929) J Am Chem Soc , vol.51 , pp. 1255-1260
    • Sumner, J.B.1    Hand, D.B.2
  • 42
    • 0001565901 scopus 로고
    • The isolation of a fourth crystallizable jack bean globulin through the digestion of canavalin with trypsin
    • Sumner J.B., and Howell S.F. The isolation of a fourth crystallizable jack bean globulin through the digestion of canavalin with trypsin. J Biol Chem 113 (1936) 607-610
    • (1936) J Biol Chem , vol.113 , pp. 607-610
    • Sumner, J.B.1    Howell, S.F.2
  • 43
    • 12444305390 scopus 로고    scopus 로고
    • Industrial crystallization developments in research and technology
    • Ulrich J., and Jones M.J. Industrial crystallization developments in research and technology. Chem Eng Res Des 82 (2004) 1567-1570
    • (2004) Chem Eng Res Des , vol.82 , pp. 1567-1570
    • Ulrich, J.1    Jones, M.J.2
  • 44
    • 41849114444 scopus 로고    scopus 로고
    • Ulrich, J. and Jones, M.J., 2006, Heat and mass transfer operations-crystallization, in Unit Operations, Pohorecki, R. (Honorary Theme Editor), (Encyclopedia of Life Support Systems (EOLSS), developed under the auspices of the UNESCO, Eolls Publishers, Oxford, UK), http://www.eolss.net.
    • Ulrich, J. and Jones, M.J., 2006, Heat and mass transfer operations-crystallization, in Unit Operations, Pohorecki, R. (Honorary Theme Editor), (Encyclopedia of Life Support Systems (EOLSS), developed under the auspices of the UNESCO, Eolls Publishers, Oxford, UK), http://www.eolss.net.
  • 46
    • 0042203975 scopus 로고    scopus 로고
    • Protein crystallization is an exacting task but can be successfully applied in industry
    • Visuri K. Protein crystallization is an exacting task but can be successfully applied in industry. Kemia-Kemi 27 (2000) 180-183
    • (2000) Kemia-Kemi , vol.27 , pp. 180-183
    • Visuri, K.1
  • 48
    • 0010602249 scopus 로고
    • Egg proteins
    • Neurath H., and Bailey K. (Eds), Academic Press Inc, New York, USA
    • Wagner R.C. Egg proteins. In: Neurath H., and Bailey K. (Eds). The Proteins, vol. II, Part A (1954), Academic Press Inc, New York, USA 435-486
    • (1954) The Proteins, vol. II, Part A , pp. 435-486
    • Wagner, R.C.1
  • 50
    • 33947332625 scopus 로고
    • Phenol-hypochlorite reaction for determination of ammonia
    • Weatherburn M.W. Phenol-hypochlorite reaction for determination of ammonia. Anal Chem 39 8 (1967) 971-974
    • (1967) Anal Chem , vol.39 , Issue.8 , pp. 971-974
    • Weatherburn, M.W.1
  • 51
    • 27344444853 scopus 로고    scopus 로고
    • Weber, M., Jones, M.J., Pietzsch, M., Hertel, T. and Ulrich, J., Purification of urease by crystallization, 2005, in VDI Berichte 1901: Proceedings of the 16th International Symposium on Industrial Crystallization, Ulrich, J. (ed) (VDI-Verlag, Düsseldorf, Germany), vol. 1, pp. 23-28.
    • Weber, M., Jones, M.J., Pietzsch, M., Hertel, T. and Ulrich, J., Purification of urease by crystallization, 2005, in VDI Berichte 1901: Proceedings of the 16th International Symposium on Industrial Crystallization, Ulrich, J. (ed) (VDI-Verlag, Düsseldorf, Germany), vol. 1, pp. 23-28.


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