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Volumn 128, Issue 3, 2007, Pages 587-596

Current status of technical protein refolding

Author keywords

Escherichia coli; Inclusion bodies; Large scale; Refolding

Indexed keywords

CELLS; ESCHERICHIA COLI; GENETIC ENGINEERING; INDUSTRIAL APPLICATIONS; MICROORGANISMS; REACTION KINETICS;

EID: 33846371209     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.12.004     Document Type: Review
Times cited : (163)

References (65)
  • 1
    • 0032965815 scopus 로고    scopus 로고
    • Oxidative refolding chromatography: folding of the scorpion toxin Cn5
    • Altamirano M.M., Garcia C., Possani L.D., and Fersht A.R. Oxidative refolding chromatography: folding of the scorpion toxin Cn5. Nat. Biotechnol. 17 (1999) 187-191
    • (1999) Nat. Biotechnol. , vol.17 , pp. 187-191
    • Altamirano, M.M.1    Garcia, C.2    Possani, L.D.3    Fersht, A.R.4
  • 3
    • 14744289727 scopus 로고
    • Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase
    • Buchner J., Brinkmann U., and Pastan I. Renaturation of a single-chain immunotoxin facilitated by chaperones and protein disulfide isomerase. Bio/Technology 10 (1992) 682-685
    • (1992) Bio/Technology , vol.10 , pp. 682-685
    • Buchner, J.1    Brinkmann, U.2    Pastan, I.3
  • 4
    • 0037071906 scopus 로고    scopus 로고
    • Construction and deconstruction of bacterial inclusion bodies
    • Carrio M.M., and Villaverde A. Construction and deconstruction of bacterial inclusion bodies. J. Biotechnol. 96 (2002) 3-12
    • (2002) J. Biotechnol. , vol.96 , pp. 3-12
    • Carrio, M.M.1    Villaverde, A.2
  • 5
    • 0019466154 scopus 로고
    • Stabilization of a degradable protein by its overexpression in Escherichia coli
    • Cheng Y.-S.E., Kwoh D.Y., Kwoh T.J., Soltvedt B.C., and Zipser D. Stabilization of a degradable protein by its overexpression in Escherichia coli. Gene 14 (1981) 121-130
    • (1981) Gene , vol.14 , pp. 121-130
    • Cheng, Y.-S.E.1    Kwoh, D.Y.2    Kwoh, T.J.3    Soltvedt, B.C.4    Zipser, D.5
  • 6
    • 0035552951 scopus 로고    scopus 로고
    • Refolding of protein inclusion bodies directly from E. coli homogenate using expanded bed adsorption chromatography
    • Cho T.H., Ahn S.J., and Lee E.K. Refolding of protein inclusion bodies directly from E. coli homogenate using expanded bed adsorption chromatography. Bioseparation 10 (2001) 189-196
    • (2001) Bioseparation , vol.10 , pp. 189-196
    • Cho, T.H.1    Ahn, S.J.2    Lee, E.K.3
  • 7
    • 27844462043 scopus 로고    scopus 로고
    • Recent advances in biomolecular process intensification
    • Choe W.-S., Nian R., and Lai W.-B. Recent advances in biomolecular process intensification. Chem. Eng. Sci. 61 (2006) 886-906
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 886-906
    • Choe, W.-S.1    Nian, R.2    Lai, W.-B.3
  • 9
    • 33846367045 scopus 로고    scopus 로고
    • Creighton, T., 1990. Process for the production of a protein. US patent 4,977,248.
  • 12
    • 0033585859 scopus 로고    scopus 로고
    • Chemical treatment of Escherichia coli. 3. Selective extraction of a recombinant protein from cytoplasmic inclusion bodies in intact cells
    • Falconer R.J., O'Neill B.K., and Middelberg A.P.J. Chemical treatment of Escherichia coli. 3. Selective extraction of a recombinant protein from cytoplasmic inclusion bodies in intact cells. Biotechnol. Bioeng. 62 (1999) 455-460
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 455-460
    • Falconer, R.J.1    O'Neill, B.K.2    Middelberg, A.P.J.3
  • 15
    • 0021659554 scopus 로고
    • Folding pathway of a circular form of bovine pancreatic trypsin inhibitor
    • Goldenberg D.P., and Creighton T.E. Folding pathway of a circular form of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 179 (1984) 527-545
    • (1984) J. Mol. Biol. , vol.179 , pp. 527-545
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 16
    • 0032574760 scopus 로고    scopus 로고
    • High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure
    • Gorovits B.M., and Horowitz P.M. High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure. Biochemistry 37 (1998) 6132-6135
    • (1998) Biochemistry , vol.37 , pp. 6132-6135
    • Gorovits, B.M.1    Horowitz, P.M.2
  • 17
    • 0025352546 scopus 로고
    • Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli
    • Hart R.A., Rinas U., and Bailey J.E. Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli. J. Biol. Chem. 265 (1990) 12728-12733
    • (1990) J. Biol. Chem. , vol.265 , pp. 12728-12733
    • Hart, R.A.1    Rinas, U.2    Bailey, J.E.3
  • 18
    • 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
  • 20
    • 0028393190 scopus 로고
    • Monitoring recombinant inclusion body recovery in an industrial disc stack centrifuge
    • Jin K., Thomas O.R.T., and Dunnill P. Monitoring recombinant inclusion body recovery in an industrial disc stack centrifuge. Biotechnol. Bioeng. 43 (1994) 455-460
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 455-460
    • Jin, K.1    Thomas, O.R.T.2    Dunnill, P.3
  • 21
    • 4644352412 scopus 로고    scopus 로고
    • Folding and refolding of proteins in chromatographic beds
    • Jungbauer A., Kaar W., and Schlegl R. Folding and refolding of proteins in chromatographic beds. Curr. Opin. Biotechnol. 15 (2004) 487-494
    • (2004) Curr. Opin. Biotechnol. , vol.15 , pp. 487-494
    • Jungbauer, A.1    Kaar, W.2    Schlegl, R.3
  • 23
    • 0032171073 scopus 로고    scopus 로고
    • Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli
    • Khan R.H., Rao K.B., Eshwari A.N., Totey S.M., and Panda A.K. Solubilization of recombinant ovine growth hormone with retention of native-like secondary structure and its refolding from the inclusion bodies of Escherichia coli. Biotechnol. Prog. 14 (1998) 722-728
    • (1998) Biotechnol. Prog. , vol.14 , pp. 722-728
    • Khan, R.H.1    Rao, K.B.2    Eshwari, A.N.3    Totey, S.M.4    Panda, A.K.5
  • 24
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber T., Rudolph R., Kohler H.H., and Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Bio/Technology 9 (1991) 825-829
    • (1991) Bio/Technology , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 25
    • 0023117045 scopus 로고
    • Intracellular degradation of recombinant proteins in relation to their location in Escherichia coli cells
    • Kitano K., Fujimoto S., and Nakao M. Intracellular degradation of recombinant proteins in relation to their location in Escherichia coli cells. J. Biotechnol. 5 (1987) 77-86
    • (1987) J. Biotechnol. , vol.5 , pp. 77-86
    • Kitano, K.1    Fujimoto, S.2    Nakao, M.3
  • 26
    • 0024633534 scopus 로고
    • Control of formation of active soluble or inactive insoluble baker's yeast α-glucosidase PI in Escherichia coli by induction and growth conditions
    • Kopetzki E., Schumacher G., and Buckel P. Control of formation of active soluble or inactive insoluble baker's yeast α-glucosidase PI in Escherichia coli by induction and growth conditions. Mol. Genet. Genomics 216 (1989) 149-155
    • (1989) Mol. Genet. Genomics , vol.216 , pp. 149-155
    • Kopetzki, E.1    Schumacher, G.2    Buckel, P.3
  • 27
    • 0037118265 scopus 로고    scopus 로고
    • The influence of mixing on lysozyme renaturation during refolding in an oscillatory flow and a stirred-tank reactor
    • Lee C.T., Buswell A.M., and Middelberg A.P.J. The influence of mixing on lysozyme renaturation during refolding in an oscillatory flow and a stirred-tank reactor. Chem. Eng. Sci. 57 (2002) 1679-1684
    • (2002) Chem. Eng. Sci. , vol.57 , pp. 1679-1684
    • Lee, C.T.1    Buswell, A.M.2    Middelberg, A.P.J.3
  • 29
    • 0347761244 scopus 로고    scopus 로고
    • Combined in-fermenter extraction and cross-flow microfiltration for improved inclusion body processing
    • Lee C.T., Morreale G., and Middelberg A.P.J. Combined in-fermenter extraction and cross-flow microfiltration for improved inclusion body processing. Biotechnol. Bioeng. 85 (2004) 103-113
    • (2004) Biotechnol. Bioeng. , vol.85 , pp. 103-113
    • Lee, C.T.1    Morreale, G.2    Middelberg, A.P.J.3
  • 30
    • 1842763662 scopus 로고    scopus 로고
    • Maximizing recovery of native protein from aggregates by optimizing pressure treatment
    • Lefebvre B.G., Gage M.J., and Robinson A.S. Maximizing recovery of native protein from aggregates by optimizing pressure treatment. Biotechnol. Prog. 20 (2004) 623-629
    • (2004) Biotechnol. Prog. , vol.20 , pp. 623-629
    • Lefebvre, B.G.1    Gage, M.J.2    Robinson, A.S.3
  • 31
    • 0037076677 scopus 로고    scopus 로고
    • Dual gradient ion-exchange chromatography improved refolding yield of lysozyme
    • Li M., Zhang G.F., and Su Z.G. Dual gradient ion-exchange chromatography improved refolding yield of lysozyme. J. Chromatogr. A 959 (2002) 113-120
    • (2002) J. Chromatogr. A , vol.959 , pp. 113-120
    • Li, M.1    Zhang, G.F.2    Su, Z.G.3
  • 32
    • 0034624223 scopus 로고    scopus 로고
    • Cycloamylose as an efficient artificial chaperone for protein refolding
    • Machida S., Ogawa S., Xiaohua S., Takaha T., Fujii K., and Hayashi K. Cycloamylose as an efficient artificial chaperone for protein refolding. FEBS Lett. 486 (2000) 131-135
    • (2000) FEBS Lett. , vol.486 , pp. 131-135
    • Machida, S.1    Ogawa, S.2    Xiaohua, S.3    Takaha, T.4    Fujii, K.5    Hayashi, K.6
  • 33
    • 20444417784 scopus 로고    scopus 로고
    • Continuous matrix assisted refolding of a-lactalbumin by ion exchange chromatography with recycling of aggregates combined with ultradiafiltration
    • Machold C., Jungbauer A., Schlegl R., and Buchinger W. Continuous matrix assisted refolding of a-lactalbumin by ion exchange chromatography with recycling of aggregates combined with ultradiafiltration. J. Chromatogr. A 1080 (2005) 29-42
    • (2005) J. Chromatogr. A , vol.1080 , pp. 29-42
    • Machold, C.1    Jungbauer, A.2    Schlegl, R.3    Buchinger, W.4
  • 36
    • 0032874214 scopus 로고    scopus 로고
    • Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing ovine growth hormone
    • Panda A.K., Khan R.H., Rao K., and Totey S.M. Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing ovine growth hormone. J. Biotechnol. 75 (1999) 161-172
    • (1999) J. Biotechnol. , vol.75 , pp. 161-172
    • Panda, A.K.1    Khan, R.H.2    Rao, K.3    Totey, S.M.4
  • 37
    • 23844540005 scopus 로고    scopus 로고
    • Development of novel protein refolding using simulated moving bed chromatography
    • Park B.-J., Koo Y.-M., and Lee C.-H. Development of novel protein refolding using simulated moving bed chromatography. Korean J. Chem. Eng. 22 (2005) 425-432
    • (2005) Korean J. Chem. Eng. , vol.22 , pp. 425-432
    • Park, B.-J.1    Koo, Y.-M.2    Lee, C.-H.3
  • 38
    • 0032905064 scopus 로고    scopus 로고
    • The production and characterisation of an immobilised chaperonin system
    • Preston N.S., Baker D.J., Bottomley S.P., and Gore M.G. The production and characterisation of an immobilised chaperonin system. Biochim. Biophys. Acta 1426 (1999) 99-109
    • (1999) Biochim. Biophys. Acta , vol.1426 , pp. 99-109
    • Preston, N.S.1    Baker, D.J.2    Bottomley, S.P.3    Gore, M.G.4
  • 39
    • 0026658065 scopus 로고
    • Solubilization of growth hormone and other recombinant proteins from Escherichia coli inclusion bodies by using a cationic surfactant
    • Puri N.K., Crivelli E., Cardamone M., Fiddes R., Bertolini J., Ninham B., and Brandon M.R. Solubilization of growth hormone and other recombinant proteins from Escherichia coli inclusion bodies by using a cationic surfactant. Biochem. J. 285 (1992) 871-879
    • (1992) Biochem. J. , vol.285 , pp. 871-879
    • Puri, N.K.1    Crivelli, E.2    Cardamone, M.3    Fiddes, R.4    Bertolini, J.5    Ninham, B.6    Brandon, M.R.7
  • 40
    • 0026605979 scopus 로고
    • Cysteine to serine substitutions in basic fibroblast growth factor: effect on inclusion body formation and proteolytic susceptibility during in vitro refolding
    • Rinas U., Tsai L.B., Lyons D., Fox G.M., Stearns G., Fieschko J., Fenton D., and Bailey J.E. Cysteine to serine substitutions in basic fibroblast growth factor: effect on inclusion body formation and proteolytic susceptibility during in vitro refolding. Bio/Technology 10 (1992) 435-440
    • (1992) Bio/Technology , vol.10 , pp. 435-440
    • Rinas, U.1    Tsai, L.B.2    Lyons, D.3    Fox, G.M.4    Stearns, G.5    Fieschko, J.6    Fenton, D.7    Bailey, J.E.8
  • 41
    • 0030041098 scopus 로고    scopus 로고
    • Artificial chaperone-assisted refolding of carbonic anhydrase B
    • Rozema D., and Gellman S.H. Artificial chaperone-assisted refolding of carbonic anhydrase B. J. Biol. Chem. 271 (1996) 3478-3487
    • (1996) J. Biol. Chem. , vol.271 , pp. 3478-3487
    • Rozema, D.1    Gellman, S.H.2
  • 42
    • 33846363581 scopus 로고    scopus 로고
    • Rudolph, R., Fischer, S., 1990. Process for Obtaining Renatured Proteins. US patent 4,933,494.
  • 43
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature
    • Schein C.H., and Noteborn M.H.M. Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature. Bio/Technology 6 (1988) 291-294
    • (1988) Bio/Technology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 45
    • 28144454566 scopus 로고    scopus 로고
    • Continuous matrix-assisted refolding of inclusion-body proteins: effect of recycling
    • Schlegl R., Necina R., and Jungbauer A. Continuous matrix-assisted refolding of inclusion-body proteins: effect of recycling. Chem. Eng. Technol. 28 (2005) 1375-1386
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 1375-1386
    • Schlegl, R.1    Necina, R.2    Jungbauer, A.3
  • 47
    • 23044453734 scopus 로고    scopus 로고
    • Reconstitution of functional nuclear receptor proteins using high pressure refolding
    • Schoner B.E., Bramlett K.S., Guo H., and Burris T.P. Reconstitution of functional nuclear receptor proteins using high pressure refolding. Mol. Genet. Metab. 85 (2005) 318-322
    • (2005) Mol. Genet. Metab. , vol.85 , pp. 318-322
    • Schoner, B.E.1    Bramlett, K.S.2    Guo, H.3    Burris, T.P.4
  • 48
    • 0021949098 scopus 로고
    • Isolation and purification of protein granules from Escherichia coli cells overproducing bovine growth hormone
    • Schoner R.G., Ellis L.F., and Schoner B.E. Isolation and purification of protein granules from Escherichia coli cells overproducing bovine growth hormone. Bio/Technology 3 (1985) 151-154
    • (1985) Bio/Technology , vol.3 , pp. 151-154
    • Schoner, R.G.1    Ellis, L.F.2    Schoner, B.E.3
  • 49
    • 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
  • 50
    • 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., and King J. Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat. Biotechnol. 14 (1996) 1283-1287
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1283-1287
    • Speed, M.A.1    Wang, D.I.C.2    King, J.3
  • 51
    • 0033539596 scopus 로고    scopus 로고
    • High pressure fosters protein refolding from aggregates at high concentrations
    • St. John R.J., Carpenter J.F., and Randolph T.W. High pressure fosters protein refolding from aggregates at high concentrations. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 13029-13033
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13029-13033
    • St. John, R.J.1    Carpenter, J.F.2    Randolph, T.W.3
  • 52
    • 0029670580 scopus 로고    scopus 로고
    • A fusion protein designed for noncovalent immobilization: stability, enzymatic activity, and use in an enzyme reactor
    • Stempfer G., HollNeugebauer B., Kopetzki E., and Rudolph R. A fusion protein designed for noncovalent immobilization: stability, enzymatic activity, and use in an enzyme reactor. Nat. Biotechnol. 14 (1996) 481-484
    • (1996) Nat. Biotechnol. , vol.14 , pp. 481-484
    • Stempfer, G.1    HollNeugebauer, B.2    Kopetzki, E.3    Rudolph, R.4
  • 53
    • 0028298199 scopus 로고
    • Procedure for refolding and purification of recombinant proteins from Escherichia coli inclusion bodies using a strong anion exchanger
    • Suttnar J., Dyr J.E., Hamsikova E., Novak J., and Vonka V. Procedure for refolding and purification of recombinant proteins from Escherichia coli inclusion bodies using a strong anion exchanger. J. Chromatogr. B 656 (1994) 123-126
    • (1994) J. Chromatogr. B , vol.656 , pp. 123-126
    • Suttnar, J.1    Dyr, J.E.2    Hamsikova, E.3    Novak, J.4    Vonka, V.5
  • 55
    • 0030019343 scopus 로고    scopus 로고
    • Effective refolding of fully reduced lysozyme with a flow-type reactor
    • Terashima M., Suzuki K., and Katoh S. Effective refolding of fully reduced lysozyme with a flow-type reactor. Process Biochem. 31 (1996) 341-345
    • (1996) Process Biochem. , vol.31 , pp. 341-345
    • Terashima, M.1    Suzuki, K.2    Katoh, S.3
  • 57
    • 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 Arakawa 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    Arakawa, T.5
  • 58
    • 0042379888 scopus 로고    scopus 로고
    • Immobilized oxidoreductase as an additive for refolding inclusion bodies: application to antibody fragments
    • Tsumoto K., Umetsu M., Yamada H., Ito T., Misawa S., and Kumagai I. Immobilized oxidoreductase as an additive for refolding inclusion bodies: application to antibody fragments. Protein Eng. 16 (2003) 535-541
    • (2003) Protein Eng. , vol.16 , pp. 535-541
    • Tsumoto, K.1    Umetsu, M.2    Yamada, H.3    Ito, T.4    Misawa, S.5    Kumagai, I.6
  • 59
    • 0013001642 scopus 로고    scopus 로고
    • How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment
    • Umetsu M., Tsumoto K., Hara M., Ashish K., Goda S., Adschiri T., and Kumagai I. How additives influence the refolding of immunoglobulin-folded proteins in a stepwise dialysis system. Spectroscopic evidence for highly efficient refolding of a single-chain Fv fragment. J. Biol. Chem. 278 (2003) 8979-8987
    • (2003) J. Biol. Chem. , vol.278 , pp. 8979-8987
    • Umetsu, M.1    Tsumoto, K.2    Hara, M.3    Ashish, K.4    Goda, S.5    Adschiri, T.6    Kumagai, I.7
  • 61
    • 14744278850 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • Wilkinson D.L., and Harrison R.G. Predicting the solubility of recombinant proteins in Escherichia coli. Bio/Technology 9 (1991) 443-448
    • (1991) Bio/Technology , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 62
    • 0030390988 scopus 로고    scopus 로고
    • Centrifugal processing of cell debris and inclusion bodies from recombinant Escherichia coli
    • Wong H.H., O'Neill B.K., and Middelberg A.P.J. Centrifugal processing of cell debris and inclusion bodies from recombinant Escherichia coli. Bioseparation 6 (1997) 361-372
    • (1997) Bioseparation , vol.6 , pp. 361-372
    • Wong, H.H.1    O'Neill, B.K.2    Middelberg, A.P.J.3
  • 63
    • 0031954924 scopus 로고    scopus 로고
    • Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry
    • Wu J., Yang Y., and Watson J.T. Trapping of intermediates during the refolding of recombinant human epidermal growth factor (hEGF) by cyanylation, and subsequent structural elucidation by mass spectrometry. Protein Sci. 7 (1998) 1017-1028
    • (1998) Protein Sci. , vol.7 , pp. 1017-1028
    • Wu, J.1    Yang, Y.2    Watson, J.T.3
  • 65
    • 0018788361 scopus 로고
    • Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation
    • Zettlmeissl G., Rudolph R., and Jaenicke 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
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3


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