메뉴 건너뛰기




Volumn 11, Issue 11, 2002, Pages 2584-2595

Immunochemical pulsed-labeling characterization of intermediates during hen lysozyme oxidative folding

Author keywords

Disulfide; ELISA; Folding kinetics; Monoclonal antibody; Reduced lysozyme

Indexed keywords

EGG WHITE; EPITOPE; LYSOZYME; MONOCLONAL ANTIBODY; GUANIDINE; HEN EGG LYSOZYME;

EID: 0036839161     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0221802     Document Type: Article
Times cited : (12)

References (34)
  • 2
    • 0017140729 scopus 로고
    • The folding pathway of reduced lysozyme
    • Anderson, W.L. and Wetlaufer, D.B. 1976. The folding pathway of reduced lysozyme. J. Biol. Chem. 251: 3147-3153.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3147-3153
    • Anderson, W.L.1    Wetlaufer, D.B.2
  • 3
    • 0035940959 scopus 로고    scopus 로고
    • Cooperative folding of the isolated α-domain of hen egg-white lysozyme
    • Bai, P. and Peng, Z. 2001. Cooperative folding of the isolated α-domain of hen egg-white lysozyme. J. Mol. Biol. 314: 321-329.
    • (2001) J. Mol. Biol. , vol.314 , pp. 321-329
    • Bai, P.1    Peng, Z.2
  • 4
    • 0013852463 scopus 로고
    • Structure of hen egg white lysozyme. A three-dimensional Fourier analysis at 2 Å resolution
    • Blake, C.C.F., Koenig, D.F., Mair, G.A., North, A.C.T., Phillips, D.C., and Sarma, V.R. 1965. Structure of hen egg white lysozyme. A three-dimensional Fourier analysis at 2 Å resolution. Nature 206: 757-761.
    • (1965) Nature , vol.206 , pp. 757-761
    • Blake, C.C.F.1    Koenig, D.F.2    Mair, G.A.3    North, A.C.T.4    Phillips, D.C.5    Sarma, V.R.6
  • 6
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote, J. and Winter, G. 1992. Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224: 487-499.
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 7
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet, B., Chaffotte, A.F., Djavadi-Ohaniance, L., and Goldberg, M.E. 1985. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods 77: 305-319.
    • (1985) J. Immunol. Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 8
    • 0021279954 scopus 로고
    • Some monoclonal antibodies raised with a native protein bind preferentially to the denatured antigen
    • Friguet, B., Djavadi-Ohaniance, L., and Goldberg, M.E. 1984. Some monoclonal antibodies raised with a native protein bind preferentially to the denatured antigen. Mol. Immunol. 21: 673-677.
    • (1984) Mol. Immunol. , vol.21 , pp. 673-677
    • Friguet, B.1    Djavadi-Ohaniance, L.2    Goldberg, M.E.3
  • 9
    • 0022904715 scopus 로고
    • 2 subunit of Escherichia coli tryptophan synthase analyzed with monoclonal antibodies
    • 2 subunit of Escherichia coli tryptophan synthase analyzed with monoclonal antibodies. Eur. J. Biochem. 160: 593-597.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 593-597
  • 10
    • 0002419595 scopus 로고
    • Immunochemial analysis of protein conformation
    • (ed. T. Creighton). IRL Press, Oxford
    • -. 1989. Immunochemial analysis of protein conformation. In Protein structure: a practical approach (ed. T. Creighton), pp. 287-310. IRL Press, Oxford.
    • (1989) Protein structure: a practical approach , pp. 287-310
  • 11
    • 0016852404 scopus 로고
    • An immunological approach to the conformational equilibrium of staphylococcal nuclease
    • Furie, B., Schechter, A.N., Sachs, D.H., and Anfinsen, C.B. 1975. An immunological approach to the conformational equilibrium of staphylococcal nuclease. J. Mol. Biol. 92: 497-506.
    • (1975) J. Mol. Biol. , vol.92 , pp. 497-506
    • Furie, B.1    Schechter, A.N.2    Sachs, D.H.3    Anfinsen, C.B.4
  • 12
    • 0028365941 scopus 로고
    • Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme
    • Goldberg, M.E. and Guillou, Y. 1994. Native disulfide bonds greatly accelerate secondary structure formation in the folding of lysozyme. Protein Sci. 3: 883-887.
    • (1994) Protein Sci. , vol.3 , pp. 883-887
    • Goldberg, M.E.1    Guillou, Y.2
  • 13
    • 0025843479 scopus 로고
    • A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysosyme
    • Goldberg, M.E., Rudolph, R., and Jaenicke, R. 1991. A kinetic study of the competition between renaturation and aggregation during the refolding of denatured-reduced egg white lysosyme. Biochemistry 30: 2790-2797.
    • (1991) Biochemistry , vol.30 , pp. 2790-2797
    • Goldberg, M.E.1    Rudolph, R.2    Jaenicke, R.3
  • 14
    • 0033522914 scopus 로고    scopus 로고
    • Pseudo-native motifs in the noncovalent heme-apocytochrome c complex: Evidence from antibody binding studies by ELISA and microcalorimetry
    • Goldberg, M.E., Schaeffer, F., Guillou, Y., and Djavadi-Ohaniance, L. 1999. Pseudo-native motifs in the noncovalent heme-apocytochrome c complex: Evidence from antibody binding studies by ELISA and microcalorimetry. J. Biol. Chem. 274: 16052-16061.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16052-16061
    • Goldberg, M.E.1    Schaeffer, F.2    Guillou, Y.3    Djavadi-Ohaniance, L.4
  • 15
    • 0036225132 scopus 로고    scopus 로고
    • Role of individual disulfide bonds in hen lysozyme early folding steps
    • Guez, V., Roux, P., Navon, A., and Goldberg, M.E. 2002. Role of individual disulfide bonds in hen lysozyme early folding steps. Protein Sci. 11: 1136-1151.
    • (2002) Protein Sci. , vol.11 , pp. 1136-1151
    • Guez, V.1    Roux, P.2    Navon, A.3    Goldberg, M.E.4
  • 16
    • 0000832134 scopus 로고
    • Protein interactions
    • (eds. H. Neurath and K. Bailey). Academic Press, New York
    • Klotz, I.M. 1953. Protein interactions. In The proteins (eds. H. Neurath and K. Bailey), pp. 727-806, vol. 1. Academic Press, New York.
    • (1953) The proteins , vol.1 , pp. 727-806
    • Klotz, I.M.1
  • 18
    • 0037133135 scopus 로고    scopus 로고
    • NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115] - A disulfide intermediate with a partly unfolded structure
    • Noda, Y., Yokota, A., Horii, D., Tominaga, T., Tankiska, Y., Tachibana, H., and Segawa, S.I. 2002. NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115] - A disulfide intermediate with a partly unfolded structure. Biochemistry 41: 2130-2139.
    • (2002) Biochemistry , vol.41 , pp. 2130-2139
    • Noda, Y.1    Yokota, A.2    Horii, D.3    Tominaga, T.4    Tankiska, Y.5    Tachibana, H.6    Segawa, S.I.7
  • 19
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates and multiple pathways
    • Radford, S.E., Dobson, C.M., and Evans, P.A. 1992. The folding of hen lysozyme involves partially structured intermediates and multiple pathways. Nature 358: 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 20
    • 0030770604 scopus 로고    scopus 로고
    • Kinetics of secondary structure recovery during the refolding of reduced hen egg white lysozyme
    • Roux, P., Delepierre, M., Goldberg, M.E., and Chaffotte, A.F. 1997. Kinetics of secondary structure recovery during the refolding of reduced hen egg white lysozyme. J. Biol. Chem. 272: 24843-24849.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24843-24849
    • Roux, P.1    Delepierre, M.2    Goldberg, M.E.3    Chaffotte, A.F.4
  • 21
    • 0033462152 scopus 로고    scopus 로고
    • Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme
    • Roux, P., Ruoppolo, M., Chaffotte, A.F., and Goldberg, M.E. 1999. Comparison of the kinetics of S-S bond, secondary structure, and active site formation during refolding of reduced denatured hen egg white lysozyme. Protein Sci. 8: 2751-2760.
    • (1999) Protein Sci. , vol.8 , pp. 2751-2760
    • Roux, P.1    Ruoppolo, M.2    Chaffotte, A.F.3    Goldberg, M.E.4
  • 22
    • 0015457562 scopus 로고
    • An immunologic approach to the conformational equilibria of polypeptides
    • Sachs, D.H., Schechter, A.N., Eastlake, A., and Anfinsen, C.B. 1972. An immunologic approach to the conformational equilibria of polypeptides. Proc. Natl. Acad Sci. 69: 3790-3794.
    • (1972) Proc. Natl. Acad Sci. , vol.69 , pp. 3790-3794
    • Sachs, D.H.1    Schechter, A.N.2    Eastlake, A.3    Anfinsen, C.B.4
  • 25
    • 0028631937 scopus 로고
    • Relationship between the optimal temperature for oxidative refolding and the thermal stability of refolded state of hen lysozyme three-disulfide derivatives
    • Tachibana, H., Ohta, Y., Sawano, H., Koumoto, Y., and Segawa, S. 1994. Relationship between the optimal temperature for oxidative refolding and the thermal stability of refolded state of hen lysozyme three-disulfide derivatives. Biochemistry 33: 15008-15016.
    • (1994) Biochemistry , vol.33 , pp. 15008-15016
    • Tachibana, H.1    Ohta, Y.2    Sawano, H.3    Koumoto, Y.4    Segawa, S.5
  • 26
    • 0035941116 scopus 로고    scopus 로고
    • Native-like tertiary structure formation in the α-domain of a hen lysozyme two-disulfide variant
    • Tachibana, H., Oka, T., and Akasaka, K. 2001. Native-like tertiary structure formation in the α-domain of a hen lysozyme two-disulfide variant. J. Mol. Biol. 314: 311-320.
    • (2001) J. Mol. Biol. , vol.314 , pp. 311-320
    • Tachibana, H.1    Oka, T.2    Akasaka, K.3
  • 29
    • 0032765075 scopus 로고    scopus 로고
    • Characterisation of the dominant oxidative folding intermediate of hen lysozyme
    • van den Berg, B., Chung, E.W., Robinson, C.V., and Dobson, C.M. 1999. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J. Mol. Biol. 290: 781-796.
    • (1999) J. Mol. Biol. , vol.290 , pp. 781-796
    • Van den Berg, B.1    Chung, E.W.2    Robinson, C.V.3    Dobson, C.M.4
  • 31
    • 0035822622 scopus 로고    scopus 로고
    • Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins
    • Welker, E., Wedemeyer, W.J., Narayan, M., and Scheraga, H.A. 2001b. Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins. Biochemistry 40: 9059-9064.
    • (2001) Biochemistry , vol.40 , pp. 9059-9064
    • Welker, E.1    Wedemeyer, W.J.2    Narayan, M.3    Scheraga, H.A.4
  • 32
    • 0030796986 scopus 로고    scopus 로고
    • Three-state model for lysozyme folding: Triangular folding mechanism with an energeticaly trapped intermediate
    • Wildegger, G. and Kiefhaber. T. 1997. Three-state model for lysozyme folding: Triangular folding mechanism with an energeticaly trapped intermediate. J. Mol. Biol. 270: 294-304.
    • (1997) J. Mol. Biol. , vol.270 , pp. 294-304
    • Wildegger, G.1    Kiefhaber, T.2
  • 33
    • 0031919676 scopus 로고    scopus 로고
    • Association and dissociation kinetics of anti-hen egg lysozyme monoclonal antibodies HyHEL-5 and HyHEL-10
    • Xavier, K.A. and Willson, R.C. 1998. Association and dissociation kinetics of anti-hen egg lysozyme monoclonal antibodies HyHEL-5 and HyHEL-10. Biophys. J. 74: 2036-2045.
    • (1998) Biophys. J. , vol.74 , pp. 2036-2045
    • Xavier, K.A.1    Willson, R.C.2
  • 34
    • 0030770571 scopus 로고    scopus 로고
    • Involvement of water molecules in the association of monoclonal antibody Hy-HEL-5 with bobwhite quail lysozyme
    • Xavier, K.A., Shick, K.A., Smith-Gill, S.J., and Willson, R.C. 1997. Involvement of water molecules in the association of monoclonal antibody Hy-HEL-5 with bobwhite quail lysozyme. Biophys. J. 73: 2116-2125.
    • (1997) Biophys. J. , vol.73 , pp. 2116-2125
    • Xavier, K.A.1    Shick, K.A.2    Smith-Gill, S.J.3    Willson, R.C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.