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Volumn 245, Issue 2, 1997, Pages 273-282

Denaturation and reactivation of dimeric human glutathione reductase: An assay for folding inhibitors

Author keywords

Antiparasitic drug; Human glutathione reductase; Peptide structure determination by NMR; Protein dimerization inhibitor; Unfolding reactivation

Indexed keywords

GLUTATHIONE REDUCTASE; GUANIDINE;

EID: 0030896991     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00273.x     Document Type: Article
Times cited : (36)

References (66)
  • 1
    • 0027087479 scopus 로고
    • Synthetic 'interface' peptides alter dimeric assembly of the HIV 1 and 2 proteases
    • Babé, L. M., Rosé, J. & Craik, C. S. (1992) Synthetic 'interface' peptides alter dimeric assembly of the HIV 1 and 2 proteases, Protein Sci. 1, 1244-1253.
    • (1992) Protein Sci. , vol.1 , pp. 1244-1253
    • Babé, L.M.1    Rosé, J.2    Craik, C.S.3
  • 3
    • 0026054730 scopus 로고
    • Protein-chemical standardization of the erythrocyte glutathione reductase activation test (EGRAC TEST). Application to hypothyroidism
    • Becker, K., Krebs, B. & Schirmer, R. H. (1991) Protein-chemical standardization of the erythrocyte glutathione reductase activation test (EGRAC TEST). Application to hypothyroidism. Int. J. Vit. Nutr. Res. 61, 180-187.
    • (1991) Int. J. Vit. Nutr. Res. , vol.61 , pp. 180-187
    • Becker, K.1    Krebs, B.2    Schirmer, R.H.3
  • 4
    • 0039801119 scopus 로고    scopus 로고
    • Glutathione reductase and thioredoxin reductase of the malarial parasite Plasmodium falciparum
    • Stevenson, K. J., Massey, V. & Williams, C. H. Jr, eds University Press, Calgary, in the press
    • Becker, K., Färber, P. M., von der Lieth, C. W. & Müller, S. (1997) Glutathione reductase and thioredoxin reductase of the malarial parasite Plasmodium falciparum, in Flavins and flavoproteins 12 (Stevenson, K. J., Massey, V. & Williams, C. H. Jr, eds) University Press, Calgary, in the press.
    • (1997) Flavins and Flavoproteins , vol.12
    • Becker, K.1    Färber, P.M.2    Von Der Lieth, C.W.3    Müller, S.4
  • 5
    • 0022343373 scopus 로고
    • 2-subunit of Escherichia coli tryptophan synthase
    • 2-subunit of Escherichia coli tryptophan synthase, J. Mol. Biol. 182, 597-606.
    • (1985) J. Mol. Biol. , vol.182 , pp. 597-606
    • Blond, S.1    Goldberg, M.E.2
  • 6
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. & Ernst, R. R. (1983) Coherence transfer by isotropic mixing: application to proton correlation spectroscopy, J. Magn. Reson. 53, 521-528.
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 8
    • 0029002115 scopus 로고
    • Stability of dimeric retroviral proteases
    • Darke, P. L. (1994) Stability of dimeric retroviral proteases, Methods Enzymol. 241, 104-127.
    • (1994) Methods Enzymol. , vol.241 , pp. 104-127
    • Darke, P.L.1
  • 9
    • 0024506337 scopus 로고
    • Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN
    • Deville-Bonne, D., Le Bras, G., Teschner, W. & Garel, J.-R. (1989) Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with KSCN, Biochemistry 28, 1917-1922.
    • (1989) Biochemistry , vol.28 , pp. 1917-1922
    • Deville-Bonne, D.1    Le Bras, G.2    Teschner, W.3    Garel, J.-R.4
  • 10
    • 0028308202 scopus 로고
    • Inhibition of human immunodeficiency virus type-1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain
    • Divita, G., Restle, T., Goody, R. S., Chermann, J.-C. & Baillon, J. G. (1994) Inhibition of human immunodeficiency virus type-1 reverse transcriptase dimerization using synthetic peptides derived from the connection domain, J. Biol. Chem. 269, 13080-13083.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13080-13083
    • Divita, G.1    Restle, T.2    Goody, R.S.3    Chermann, J.-C.4    Baillon, J.G.5
  • 11
    • 0028964233 scopus 로고
    • Dimerization kinetics of HIV-1 and HIV-2 reverse transcriptase: A two step process
    • Divita, G., Rittinger, K., Geourjon, C., Deléage, G. & Goody, R. S. (1995) Dimerization kinetics of HIV-1 and HIV-2 reverse transcriptase: a two step process, J. Mol. Biol. 245, 508-521.
    • (1995) J. Mol. Biol. , vol.245 , pp. 508-521
    • Divita, G.1    Rittinger, K.2    Geourjon, C.3    Deléage, G.4    Goody, R.S.5
  • 12
    • 0002258696 scopus 로고
    • Specific volumes of biological macromolecules and some other molecules of biological interest
    • Hinz, H.-J., ed. Springer-Verlag, Berlin, New York
    • Durchschlag, H. (1986) Specific volumes of biological macromolecules and some other molecules of biological interest, in Thermodynamic data for biochemistry and biotechnology (Hinz, H.-J., ed.) pp. 45-128, Springer-Verlag, Berlin, New York.
    • (1986) Thermodynamic Data for Biochemistry and Biotechnology , pp. 45-128
    • Durchschlag, H.1
  • 13
    • 0015813630 scopus 로고
    • Spectrophotometric determination of protein concentration in cell extracts containing tRNAs and rRNAs
    • Ehresmann, B., Imbault, P. & Weil, J. H. (1973) Spectrophotometric determination of protein concentration in cell extracts containing tRNAs and rRNAs, Anal. Biochem. 54, 454-463.
    • (1973) Anal. Biochem. , vol.54 , pp. 454-463
    • Ehresmann, B.1    Imbault, P.2    Weil, J.H.3
  • 14
    • 0029908565 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum
    • Färber, P. M., Becker, K., Müller, S., Schirmer, R. H. & Franklin, R. M. (1996) Molecular cloning and characterization of a putative glutathione reductase gene, the PfGR2 gene, from Plasmodium falciparum, Eur. J. Biochem. 239, 655-661.
    • (1996) Eur. J. Biochem. , vol.239 , pp. 655-661
    • Färber, P.M.1    Becker, K.2    Müller, S.3    Schirmer, R.H.4    Franklin, R.M.5
  • 15
    • 0029142578 scopus 로고
    • Cloning and sequencing of a human thioredoxin reductase
    • Gasdaska, P. Y., Gasdaska, J. R., Cochran, S. & Powis, G. (1995) Cloning and sequencing of a human thioredoxin reductase, FEBS Lett. 373, 5-9.
    • (1995) FEBS Lett. , vol.373 , pp. 5-9
    • Gasdaska, P.Y.1    Gasdaska, J.R.2    Cochran, S.3    Powis, G.4
  • 16
    • 0025194256 scopus 로고
    • Interference with the assembly of virus-host transcription complex by peptide competition
    • Haigh, A., Greaves, R. & O'Hare, P. (1990) Interference with the assembly of virus-host transcription complex by peptide competition, Nature 344, 257-259.
    • (1990) Nature , vol.344 , pp. 257-259
    • Haigh, A.1    Greaves, R.2    O'Hare, P.3
  • 17
    • 0023663689 scopus 로고
    • Hydrophobic stabilization of chiton hemocyanins: Effects of urea, Hofmeister salts and pH on their dissociation
    • Herskovits, T. T. & Hamilton, M. G. (1987) Hydrophobic stabilization of chiton hemocyanins: Effects of urea, Hofmeister salts and pH on their dissociation, Biochim. Biophys. Acta 915, 157-167.
    • (1987) Biochim. Biophys. Acta , vol.915 , pp. 157-167
    • Herskovits, T.T.1    Hamilton, M.G.2
  • 18
    • 0022555883 scopus 로고
    • Refolding and association of oligomeric proteins
    • Jaenicke, R. & Rudolph, R. (1986) Refolding and association of oligomeric proteins, Methods Enzymol. 131, 218-250.
    • (1986) Methods Enzymol. , vol.131 , pp. 218-250
    • Jaenicke, R.1    Rudolph, R.2
  • 19
    • 0025876740 scopus 로고
    • Protein folding: Local structures, domains, subunits and assemblies
    • Jaenicke, R. (1991) Protein folding: local structures, domains, subunits and assemblies, Biochemistry 30, 3147-3161.
    • (1991) Biochemistry , vol.30 , pp. 3147-3161
    • Jaenicke, R.1
  • 20
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, B. H., Bachmann, P. & Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy, J. Chem. Phys. 71, 4546-4553.
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 22
    • 0023644992 scopus 로고
    • Refined structure of glutathione reductase at 1.54 Å resolution
    • Karplus, P. A. & Schulz, G. E. (1987) Refined structure of glutathione reductase at 1.54 Å resolution, J. Mol. Biol. 195, 701-729.
    • (1987) J. Mol. Biol. , vol.195 , pp. 701-729
    • Karplus, P.A.1    Schulz, G.E.2
  • 23
    • 0014010861 scopus 로고
    • Viscosity and density of aqueous solutions of urea and guanidine hydrochloride
    • Kawahara, K. & Tanford, C. (1966) Viscosity and density of aqueous solutions of urea and guanidine hydrochloride, J. Biol. Chem. 241, 3228-3232.
    • (1966) J. Biol. Chem. , vol.241 , pp. 3228-3232
    • Kawahara, K.1    Tanford, C.2
  • 24
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • in the press
    • Koradi, R., Billeter, M. & Wüthrich, K. (1997) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, in the press.
    • (1997) J. Mol. Graphics , vol.14
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 26
    • 0029360570 scopus 로고
    • Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design
    • Krauth-Siegel, R. L. & Schöneck, R. (1995) Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design, FASEB J. 9, 1138-1146.
    • (1995) FASEB J. , vol.9 , pp. 1138-1146
    • Krauth-Siegel, R.L.1    Schöneck, R.2
  • 27
    • 0017760360 scopus 로고
    • Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide
    • Krohne-Ehrich, G., Schirmer, R. H. & Untucht-Grau, R. (1977) Glutathione reductase from human erythrocytes. Isolation of the enzyme and sequence analysis of the redox-active peptide, Eur. J. Biochem. 80, 65-71.
    • (1977) Eur. J. Biochem. , vol.80 , pp. 65-71
    • Krohne-Ehrich, G.1    Schirmer, R.H.2    Untucht-Grau, R.3
  • 28
    • 0027240443 scopus 로고
    • Kinetic assay for HIV proteinase subunit dissociation
    • Kuzmic, P. (1993) Kinetic assay for HIV proteinase subunit dissociation, Biochem. Biophys. Res. Commun. 191, 998-1003.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 998-1003
    • Kuzmic, P.1
  • 29
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. & Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 30
    • 0028295554 scopus 로고
    • Solubilizing buried domains of proteins: A self-assembling interface domain from glutathione reductase
    • Leistler, B. & Perham, R. N. (1994) Solubilizing buried domains of proteins: A self-assembling interface domain from glutathione reductase, Biochemistry 33, 2773-2781.
    • (1994) Biochemistry , vol.33 , pp. 2773-2781
    • Leistler, B.1    Perham, R.N.2
  • 34
    • 0023857667 scopus 로고
    • Oligopeptides inhibit the ribonucleotide reductase of herpes simplex virus by causing subunit separation
    • McClements, W., Yamanaka, G., Garsky, V., Perry, H., Bacchetti, S., Colonno, R. & Stein, R. B. (1988) Oligopeptides inhibit the ribonucleotide reductase of herpes simplex virus by causing subunit separation, Virology 162, 270-273.
    • (1988) Virology , vol.162 , pp. 270-273
    • McClements, W.1    Yamanaka, G.2    Garsky, V.3    Perry, H.4    Bacchetti, S.5    Colonno, R.6    Stein, R.B.7
  • 35
    • 0028969671 scopus 로고
    • Dissecting titin into its structural motifs: Identification of an α-helix motif near the titin N-terminus
    • Musco, G., Tziatzios, C., Schuck, P. & Pastore, A. (1995) Dissecting titin into its structural motifs: identification of an α-helix motif near the titin N-terminus, Biochemistry 34, 553-561.
    • (1995) Biochemistry , vol.34 , pp. 553-561
    • Musco, G.1    Tziatzios, C.2    Schuck, P.3    Pastore, A.4
  • 37
    • 0027190591 scopus 로고
    • Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs
    • Nordhoff, A., Bücheler, U. S., Werner, D. & Schirmer, R. H. (1993) Folding of the four domains and dimerization are impaired by the Gly446→Glu exchange in human glutathione reductase. Implications for the design of antiparasitic drugs, Biochemistry 32, 4060-4066.
    • (1993) Biochemistry , vol.32 , pp. 4060-4066
    • Nordhoff, A.1    Bücheler, U.S.2    Werner, D.3    Schirmer, R.H.4
  • 39
    • 8244253916 scopus 로고    scopus 로고
    • Denaturation and reactivation of the FAD enzyme glutathione reductase
    • Stevenson, K. J., Massey, V. & Williams, C. H. Jr, eds University Press, Calgary, in the press
    • Nordhoff, A., Becker, K., Schirmer, R. H., Tzatzios, C., van den Broek, J. A. & Schubert, D. (1997) Denaturation and reactivation of the FAD enzyme glutathione reductase, in Flavins and flavoproteins 12 (Stevenson, K. J., Massey, V. & Williams, C. H. Jr, eds) University Press, Calgary, in the press.
    • (1997) Flavins and Flavoproteins , vol.12
    • Nordhoff, A.1    Becker, K.2    Schirmer, R.H.3    Tzatzios, C.4    Van Den Broek, J.A.5    Schubert, D.6
  • 40
    • 0014226043 scopus 로고
    • Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55 degrees
    • Pace, C. N. & Tanford, C. (1968) Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55 degrees, Biochemistry 7, 198-208.
    • (1968) Biochemistry , vol.7 , pp. 198-208
    • Pace, C.N.1    Tanford, C.2
  • 42
    • 0030032964 scopus 로고    scopus 로고
    • Protein engineering of domains in flavoprotein disulphide oxidoreductases: Contributions to folding and assembly
    • Perham, R. N., Leistler, B., Solomon, R. G. & Guptasarma, P. (1996) Protein engineering of domains in flavoprotein disulphide oxidoreductases: contributions to folding and assembly, Biochem. Soc. Trans. 24, 61-66.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 61-66
    • Perham, R.N.1    Leistler, B.2    Solomon, R.G.3    Guptasarma, P.4
  • 43
    • 0027534686 scopus 로고
    • Renaturation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides after denaturation in 4 M guanidine hydrochloride: Kinetics of aggregation and reactivation
    • Plomer, J. J. & Gafni, A. (1993) Renaturation of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides after denaturation in 4 M guanidine hydrochloride: kinetics of aggregation and reactivation, Biochem. Biophys. Acta 1163, 89-96.
    • (1993) Biochem. Biophys. Acta , vol.1163 , pp. 89-96
    • Plomer, J.J.1    Gafni, A.2
  • 46
    • 0027069576 scopus 로고
    • Stability and reconstitution of pyruvate oxidase from Lactobacillus plantarum: Dissection of the stabilizing effects of coenzyme binding and subunit interaction
    • Risse, B., Stempfer, G., Rudolph, R., Möllering, H. & Jaenicke, R. (1992) Stability and reconstitution of pyruvate oxidase from Lactobacillus plantarum: dissection of the stabilizing effects of coenzyme binding and subunit interaction, Protein Sci. 1, 1699-1709.
    • (1992) Protein Sci. , vol.1 , pp. 1699-1709
    • Risse, B.1    Stempfer, G.2    Rudolph, R.3    Möllering, H.4    Jaenicke, R.5
  • 47
    • 0027181988 scopus 로고
    • Multiphasic denaturation of glutathione transferase B1-1 by guanidinium chloride. Role of the dimeric structure on the flexibility of the active site
    • Sacchetta, P., Aceto, A., Bucciarelli, T., Dragani, B., Santarone, S., Allocati, N. & Di Ilio, C. (1993) Multiphasic denaturation of glutathione transferase B1-1 by guanidinium chloride. Role of the dimeric structure on the flexibility of the active site, Eur. J. Biochem. 215, 741-745.
    • (1993) Eur. J. Biochem. , vol.215 , pp. 741-745
    • Sacchetta, P.1    Aceto, A.2    Bucciarelli, T.3    Dragani, B.4    Santarone, S.5    Allocati, N.6    Di Ilio, C.7
  • 48
    • 33748233963 scopus 로고
    • Disulfide-reductase inhibitors as chemotherapeutic agents: The design of drugs for trypanosomiasis and malaria
    • Schirmer, R. H., Müller, J. G. & Krauth-Siegel, R. L. (1995) Disulfide-reductase inhibitors as chemotherapeutic agents: the design of drugs for trypanosomiasis and malaria, Angew. Chem. Int. Ed. Engl. 34, 141-154.
    • (1995) Angew. Chem. Int. Ed. Engl. , vol.34 , pp. 141-154
    • Schirmer, R.H.1    Müller, J.G.2    Krauth-Siegel, R.L.3
  • 50
    • 0003068117 scopus 로고
    • Analytical ultracentrifugation as a tool for studying membrane proteins
    • Schubert, D. & Schuck, P. (1991) Analytical ultracentrifugation as a tool for studying membrane proteins, Prog. Colloid Polym. Sci. 86, 12-22.
    • (1991) Prog. Colloid Polym. Sci. , vol.86 , pp. 12-22
    • Schubert, D.1    Schuck, P.2
  • 51
    • 0027928436 scopus 로고
    • Simultaneous radial and wavelength analysis with the Optima XL-A analytical ultracentrifuge
    • Schuck, P. (1994) Simultaneous radial and wavelength analysis with the Optima XL-A analytical ultracentrifuge, Prog. Colloid Polym. Sci. 94, 1-13.
    • (1994) Prog. Colloid Polym. Sci. , vol.94 , pp. 1-13
    • Schuck, P.1
  • 53
    • 0026596758 scopus 로고
    • Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor
    • Tasayco, M. & Carey, J. (1992) Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor, Science 255, 594-597.
    • (1992) Science , vol.255 , pp. 594-597
    • Tasayco, M.1    Carey, J.2
  • 54
    • 0019882046 scopus 로고
    • Three-dimensional structure of glutathione reductase at 2 Å resolution
    • Thieme, R., Pai, E. F., Schirmer, R. H. & Schulz, G. E. (1981) Three-dimensional structure of glutathione reductase at 2 Å resolution, J. Mol. Biol. 152, 763-782.
    • (1981) J. Mol. Biol. , vol.152 , pp. 763-782
    • Thieme, R.1    Pai, E.F.2    Schirmer, R.H.3    Schulz, G.E.4
  • 55
    • 0024257933 scopus 로고
    • Large-scale preparation and reconstitution of apo-flavoproteins with special reference to butyryl-CoA dehydrogenase from Magasphaera elsdenii
    • van Berkel, W. J. H., van den Berg, W. A. M. & Müller, F. (1988) Large-scale preparation and reconstitution of apo-flavoproteins with special reference to butyryl-CoA dehydrogenase from Magasphaera elsdenii, Eur. J. Biochem. 178, 197-207.
    • (1988) Eur. J. Biochem. , vol.178 , pp. 197-207
    • Van Berkel, W.J.H.1    Van Den Berg, W.A.M.2    Müller, F.3
  • 56
    • 0026343117 scopus 로고
    • The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii
    • van Berkel, W. J. H., Regelink, A. G., Beintema, J. J. & de Kok, A. (1991) The conformational stability of the redox states of lipoamide dehydrogenase from Azotobacter vinelandii, Eur. J. Biochem. 202, 1049-1055.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 1049-1055
    • Van Berkel, W.J.H.1    Regelink, A.G.2    Beintema, J.J.3    De Kok, A.4
  • 57
    • 0000876731 scopus 로고
    • Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - A family of flavoenzyme transhydrogenases
    • Müller, F., ed. CRC Press, Boca Raton FL
    • Williams, C. H. Jr (1992) Lipoamide dehydrogenase, glutathione reductase, thioredoxin reductase, and mercuric ion reductase - a family of flavoenzyme transhydrogenases, in Chemistry and biochemistry of flavoenzymes (Müller, F., ed.) vol. III, pp. 121-211, CRC Press, Boca Raton FL.
    • (1992) Chemistry and Biochemistry of Flavoenzymes , vol.3 , pp. 121-211
    • Williams Jr., C.H.1
  • 58
    • 33748241762 scopus 로고    scopus 로고
    • Control of the structure and function of biomaterials by light
    • Wilner, I. & Rubin, S. (1996) Control of the structure and function of biomaterials by light, Angew. Chem. Int. Ed. Engl. 35, 367-385.
    • (1996) Angew. Chem. Int. Ed. Engl. , vol.35 , pp. 367-385
    • Wilner, I.1    Rubin, S.2
  • 62
    • 0017165455 scopus 로고
    • Glutathione reductase from human erythrocytes. Catalytic properties and aggregation
    • Worthington, D. J. & Rosemeyer, M. A. (1976) Glutathione reductase from human erythrocytes. Catalytic properties and aggregation, Eur. J. Biochem. 67, 231-238.
    • (1976) Eur. J. Biochem. , vol.67 , pp. 231-238
    • Worthington, D.J.1    Rosemeyer, M.A.2
  • 64
    • 0020164668 scopus 로고
    • The yield of reactivation of lactic dehydrogenase after guanidine-HCl denaturation is not determined by proline cis-trans isomerization
    • Zettlmeissl, G., Rudolph, R. & Jaenicke, R. (1982) The yield of reactivation of lactic dehydrogenase after guanidine-HCl denaturation is not determined by proline cis-trans isomerization, Eur. J. Biochem. 125, 605-608.
    • (1982) Eur. J. Biochem. , vol.125 , pp. 605-608
    • Zettlmeissl, G.1    Rudolph, R.2    Jaenicke, R.3
  • 66
    • 0027062923 scopus 로고
    • Renaturation of citrate synthase: Influence of denaturant and folding assistants
    • Zhi, W., Landry, S. J., Gierasch, L. M. & Srere, P. A. (1992) Renaturation of citrate synthase: influence of denaturant and folding assistants, Protein Sci. 1, 522-529.
    • (1992) Protein Sci. , vol.1 , pp. 522-529
    • Zhi, W.1    Landry, S.J.2    Gierasch, L.M.3    Srere, P.A.4


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