메뉴 건너뛰기




Volumn 51, Issue 2, 2007, Pages 235-242

A newly proposed mechanism for arginine-assisted protein refolding-not inhibiting soluble oligomers although promoting a correct structure

Author keywords

Additives; Arginine; Recombinant consensus interferon; Refolding

Indexed keywords

ARGININE; CONSENSUS INTERFERON; RECOMBINANT INTERFERON;

EID: 33751430438     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.07.001     Document Type: Article
Times cited : (28)

References (36)
  • 1
    • 0036772580 scopus 로고    scopus 로고
    • Preparative protein refolding
    • Middelberg A.P.J. Preparative protein refolding. Trends Biotechnol. 20 (2002) 437-443
    • (2002) Trends Biotechnol. , vol.20 , pp. 437-443
    • Middelberg, A.P.J.1
  • 3
    • 0035313135 scopus 로고    scopus 로고
    • Protein refolding for industrial processes
    • De Bernardez Clark E. Protein refolding for industrial processes. Curr. Opin. Biotechnol. 12 (2001) 202-207
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 202-207
    • De Bernardez Clark, E.1
  • 4
    • 0345636051 scopus 로고    scopus 로고
    • Practical considerations in refolding proteins from inclusion bodies
    • Tsumoto K., Ejima D., Kumagai I., and Arakawa T. Practical considerations in refolding proteins from inclusion bodies. Protein Expres. Purif. 28 (2003) 1-8
    • (2003) Protein Expres. Purif. , vol.28 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4
  • 5
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen C.B. Principles that govern the folding of protein chains. Science 181 (1973) 223-230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 6
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase: noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation
    • Zettlmei G., and Rudolph R. Reconstitution of lactic dehydrogenase: noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. Biochemistry 18 (1979) 5567-5571
    • (1979) Biochemistry , vol.18 , pp. 5567-5571
    • Zettlmei, G.1    Rudolph, R.2
  • 7
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme
    • Goldberg M.E., Rudolph R., and Jaenicke R. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysozyme. Biochemistry 30 (1991) 2790-2797
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 8
    • 0026770746 scopus 로고
    • Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B: reaction stoichiometry and refolding model
    • Cleland J.L., Hedgepeth C., and Wang D.I.C. Polyethylene glycol enhanced refolding of bovine carbonic anhydrase B: reaction stoichiometry and refolding model. J. Biol. Chem. 267 (1992) 13327-13334
    • (1992) J. Biol. Chem. , vol.267 , pp. 13327-13334
    • Cleland, J.L.1    Hedgepeth, C.2    Wang, D.I.C.3
  • 10
    • 0037174127 scopus 로고    scopus 로고
    • Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichiia coli
    • Asano R., Kudo T., Makabe K., Tsumoto K., and Kumagai I. Antitumor activity of interleukin-21 prepared by novel refolding procedure from inclusion bodies expressed in Escherichiia coli. FEBS Lett. 528 (2002) 70-76
    • (2002) FEBS Lett. , vol.528 , pp. 70-76
    • Asano, R.1    Kudo, T.2    Makabe, K.3    Tsumoto, K.4    Kumagai, I.5
  • 11
    • 1642273005 scopus 로고    scopus 로고
    • Development of a biotin mimic tagged ScFv antibody against western equine encephalitis virus: bacterial and refolding
    • Dasa D., Kriangkum J., Nagata L.P., Fulton R.E., and Suresh M.R. Development of a biotin mimic tagged ScFv antibody against western equine encephalitis virus: bacterial and refolding. J. Virol. Meth. 117 (2004) 169-177
    • (2004) J. Virol. Meth. , vol.117 , pp. 169-177
    • Dasa, D.1    Kriangkum, J.2    Nagata, L.P.3    Fulton, R.E.4    Suresh, M.R.5
  • 13
    • 14744269612 scopus 로고
    • Cosolvent assisted protein refolding
    • Cleland J.L., and Wang D.I.C. Cosolvent assisted protein refolding. Biotechnology 8 (1990) 1274-1278
    • (1990) Biotechnology , vol.8 , pp. 1274-1278
    • Cleland, J.L.1    Wang, D.I.C.2
  • 14
    • 0344495223 scopus 로고    scopus 로고
    • Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine
    • Tsumoto K., Umetsu M., Kumagai I., Ejima D., and Arakaw T. Solubilization of active green fluorescent protein from insoluble particles by guanidine and arginine. Biochem. Biophys. Res. Commun. 312 (2003) 1383-1386
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 1383-1386
    • Tsumoto, K.1    Umetsu, M.2    Kumagai, I.3    Ejima, D.4    Arakaw, T.5
  • 15
    • 0020477017 scopus 로고
    • Stabilization of protein structure by sugars
    • Arakawa T., and Timasheff S.N. Stabilization of protein structure by sugars. Biochemistry 21 (1982) 6536-6544
    • (1982) Biochemistry , vol.21 , pp. 6536-6544
    • Arakawa, T.1    Timasheff, S.N.2
  • 16
    • 0019872622 scopus 로고
    • Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures
    • Gekko K., and Timasheff S.N. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 20 (1981) 4667-4676
    • (1981) Biochemistry , vol.20 , pp. 4667-4676
    • Gekko, K.1    Timasheff, S.N.2
  • 17
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly refolded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner J., Pastan I., and Brinkmann U. A method for increasing the yield of properly refolded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem. 205 (1992) 263-270
    • (1992) Anal. Biochem. , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 18
    • 0030579519 scopus 로고    scopus 로고
    • Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies
    • Arora D., and Khanna N. Method for increasing the yield of properly folded recombinant human gamma interferon from inclusion bodies. J. Biotechnol. 52 (1996) 127-133
    • (1996) J. Biotechnol. , vol.52 , pp. 127-133
    • Arora, D.1    Khanna, N.2
  • 19
    • 3543071755 scopus 로고    scopus 로고
    • Purification, refolding, and characterization of recombinant LHRH-T multimer
    • Raina K., Panda A.K., Ali M.M., and Talwar G.P. Purification, refolding, and characterization of recombinant LHRH-T multimer. Protein Expres. Purif. 37 (2004) 8-17
    • (2004) Protein Expres. Purif. , vol.37 , pp. 8-17
    • Raina, K.1    Panda, A.K.2    Ali, M.M.3    Talwar, G.P.4
  • 20
    • 2642580087 scopus 로고    scopus 로고
    • Isolation of aminoglycoside nucleotidyltransferase(200)-Ia from inclusion bodies as active, monomeric enzyme
    • Wright E., and Serpersu E.H. Isolation of aminoglycoside nucleotidyltransferase(200)-Ia from inclusion bodies as active, monomeric enzyme. Protein Expres. Purif. 35 (2004) 373-380
    • (2004) Protein Expres. Purif. , vol.35 , pp. 373-380
    • Wright, E.1    Serpersu, E.H.2
  • 21
    • 0037466513 scopus 로고    scopus 로고
    • The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation
    • Arakawa T., and Tsumoto K. The effects of arginine on refolding of aggregated proteins: not facilitate refolding, but suppress aggregation. Biochem. Biophys. Res. Commun. 304 (2003) 148-152
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 148-152
    • Arakawa, T.1    Tsumoto, K.2
  • 22
    • 15244343628 scopus 로고    scopus 로고
    • l-arginine increases the solubility of unfolded species of hen egg white lysozyme
    • Reddy K.R.C., Lilie H., Rudolph R., and Lange C. l-arginine increases the solubility of unfolded species of hen egg white lysozyme. Protein Sci. 14 (2005) 929-935
    • (2005) Protein Sci. , vol.14 , pp. 929-935
    • Reddy, K.R.C.1    Lilie, H.2    Rudolph, R.3    Lange, C.4
  • 24
    • 0025021579 scopus 로고
    • Isolation and structure characterization of three isoforms of recombinant consensus alpha interferon
    • Klein M.L., Bartley T.D., Davis J.M., Whiteley D.W., and Lu H.S. Isolation and structure characterization of three isoforms of recombinant consensus alpha interferon. Arch. Biochem. Biophys. 276 (1990) 531-537
    • (1990) Arch. Biochem. Biophys. , vol.276 , pp. 531-537
    • Klein, M.L.1    Bartley, T.D.2    Davis, J.M.3    Whiteley, D.W.4    Lu, H.S.5
  • 26
    • 0029833999 scopus 로고    scopus 로고
    • The biologic activity and molecular characterization of a novel synthetic interferon-alpha species: consensus interferon
    • Blatt L.M. The biologic activity and molecular characterization of a novel synthetic interferon-alpha species: consensus interferon. J. Interferon Cytokine Res. 16 (1996) 489-499
    • (1996) J. Interferon Cytokine Res. , vol.16 , pp. 489-499
    • Blatt, L.M.1
  • 27
    • 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., Mcrorie R.A., and Williams W.L. 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    Mcrorie, R.A.2    Williams, W.L.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0031884621 scopus 로고    scopus 로고
    • Oxidative renaturation of hen egg-white lysozyme: folding vs aggregation
    • De Bernardez Clark E., Hevehan D., Szela S., and Reddy J.M. Oxidative renaturation of hen egg-white lysozyme: folding vs aggregation. Biotechnol. Prog. 14 (1998) 47-54
    • (1998) Biotechnol. Prog. , vol.14 , pp. 47-54
    • De Bernardez Clark, E.1    Hevehan, D.2    Szela, S.3    Reddy, J.M.4
  • 30
    • 33751434633 scopus 로고    scopus 로고
    • Separation of correctly refolded and mis-refolded consensus interferon by hydrophobic interaction chromatography
    • Zhao R.Z., Liu Y.D., Wang F.W., Li J.J., Xia X., and Su Z.G. Separation of correctly refolded and mis-refolded consensus interferon by hydrophobic interaction chromatography. Chin. J. Biotechnol. 21 (2005) 451-455
    • (2005) Chin. J. Biotechnol. , vol.21 , pp. 451-455
    • Zhao, R.Z.1    Liu, Y.D.2    Wang, F.W.3    Li, J.J.4    Xia, X.5    Su, Z.G.6
  • 31
    • 0019428529 scopus 로고
    • Assignment of the disulfide bonds of leukocyte interferon
    • Wetzel R. Assignment of the disulfide bonds of leukocyte interferon. Nature 289 (1981) 606-607
    • (1981) Nature , vol.289 , pp. 606-607
    • Wetzel, R.1
  • 32
    • 0037907479 scopus 로고    scopus 로고
    • Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride
    • Srinivas V., Raman B., Rao K.S., Ramakrishna T., and Rao C.M. Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride. Protein Sci. 12 (2003) 1262-1270
    • (2003) Protein Sci. , vol.12 , pp. 1262-1270
    • Srinivas, V.1    Raman, B.2    Rao, K.S.3    Ramakrishna, T.4    Rao, C.M.5
  • 33
    • 0037502289 scopus 로고    scopus 로고
    • Separation and identification of different refolding components
    • Li M., and Su Z.G. Separation and identification of different refolding components. J. Biotechnol. 103 (2003) 119-127
    • (2003) J. Biotechnol. , vol.103 , pp. 119-127
    • Li, M.1    Su, Z.G.2
  • 34
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • Hevehan D.L., and De Bernardez Clark E. Oxidative renaturation of lysozyme at high concentrations. Biotechnol. Bioeng. 54 (1997) 221-230
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 221-230
    • Hevehan, D.L.1    De Bernardez Clark, E.2
  • 35
    • 0031688064 scopus 로고    scopus 로고
    • Renaturation of recombinant human neurotrophin-3 from inclusion bodies using an aggregation suppressor
    • Suenaga M., Ohmae H., Tsuji S., Itoh T., and Nishimura O. Renaturation of recombinant human neurotrophin-3 from inclusion bodies using an aggregation suppressor. Biotechnol. Appl. Biochem. 28 (1998) 119-124
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , pp. 119-124
    • Suenaga, M.1    Ohmae, H.2    Tsuji, S.3    Itoh, T.4    Nishimura, O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.