Complete refolding of bovine β-lactoglobulin requires disulfide bond formation under strict conditions

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1752, Issue 2, 2005, Pages 154-165

  Hattori, Makoto ^a   Hiramatsu, Kazuhiko ^a   Kurata, Takashi ^a   Nishiura, Mika ^a   Takahashi, Koji ^a   Ametani, Akio ^b   Kaminogawa, Shuichi ^b,c  

^a TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^b UNIVERSITY OF TOKYO   (Japan)

^c NIHON UNIVERSITY   (Japan)

Author keywords

Lactoglobulin; Disulfide bond formation; Refolding

Indexed keywords

BETA LACTOGLOBULIN; CHAPERONE; GUANIDINE; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN; REDUCING AGENT; RETINOL; THIOL DERIVATIVE;

ARTICLE; CIRCULAR DICHROISM; DENATURATION; DILUTION; DISULFIDE BOND; EVALUATION; FLUORESCENCE; GEL MOBILITY SHIFT ASSAY; HYDROPHILICITY; IN VITRO STUDY; METHODOLOGY; MOLECULE; NONHUMAN; OXIDATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN FOLDING; RENATURATION;

ANIMALS; ANTIBODIES, MONOCLONAL; CATTLE; DISULFIDES; DITHIONITROBENZOIC ACID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ENZYME-LINKED IMMUNOSORBENT ASSAY; GUANIDINE; LACTOGLOBULINS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE;

BOVINAE;

EID: 25144519046     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.07.015     Document Type: Article

References (35)

1. E. De Bernardez Clark Protein refolding for industrial processes Curr. Opin. Biotechnol. 12 2001 202 207
2. M. Hattori, A. Ametani, Y. Katakura, M. Shimizu, and S. Kaminogawa Unfolding/refolding studies on bovine β-lactoglobulin with monoclonal antibodies as probes. Does a renatured protein completely refold? J. Biol. Chem. 268 1993 22414 22419
3. V. Subramaniam, D.G. Steel, and A. Gafni In vitro renaturation of bovine β-lactoglobulin A leads to a biologically active but incompletely refolded state Protein Sci. 5 1996 2089 2094
4. H.A. McKenzie β-Lactoglobulins H.A. McKenzie Milk Proteins: Chemistry and Molecular Biology vol. 2 1971 Academic Press New York 257 330
5. M.Z. Papiz, L. Sawyer, E.E. Eliopoulos, A.C.T. North, J.B.C. Findlay, R. Sivaprasadrao, T.A. Jones, M.E. Newcomer, and P.J. Kraulis The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein Nature 324 1986 383 385
6. S. Brownlow, C.J. Morais, R. Cooper, D.R. Flower, S.J. Yewdall, I. Polikarpov, A.C. North, and L. Sawyer Bovine β-lactoglobulin at 1.8 Å resolution-Still an enigmatic lipocalin Structure 5 1997 481 495
7. B.Y. Qin, M.C. Bewley, L.K. Creamer, H.M. Baker, E.N. Baker, and G.B. Jameson Structural basis of the Tanford transition of bovine β-lactoglobulin Biochemistry 37 1998 14014 14023
8. B.Y. Qin, M.C. Bewley, L.K. Creamer, E.N. Baker, and G.B. Jameson Functional implications of structural differences between variants A and B of bovine β-lactoglobulin Protein Sci. 8 1999 75 83
9. K. Kuwata, M. Hoshino, V. Forge, S. Era, C.A. Batt, and Y. Goto Solution structure and dynamics of bovine β-lactoglobulin A Protein Sci. 8 1999 2541 2545
10. L. Ragona, F. Fogolari, S. Romagnoli, L. Zetta, J.L. Maubois, and H. Molinari Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements J. Mol. Biol. 293 1999 953 969
11. K. Kuwata, R. Shastry, H. Cheng, M. Hoshino, C.A. Batt, Y. Goto, and H. Roder Structural and kinetic characterization of early folding events in β-lactoglobulin Nat. Struct. Biol. 8 2001 151 155
12. D.R. Flower The lipocalin protein family: structure and function Biochem. J. 318 1996 1 14
13. L. Sawyer, and G. Kontopidis The core lipocalin, bovine β-lactoglobulin Biochim. Biophys. Acta 1482 2000 136 138
14. M.D. Pérez, and M. Calvo Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein J. Dairy Sci. 78 1995 978 988
15. S. Kaminogawa, M. Shimizu, A. Ametani, M. Hattori, O. Ando, S. Hachimura, Y. Nakamura, M. Totsuka, and K. Yamauchi Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin Biochim. Biophys. Acta 998 1989 50 56
16. A. Laligant, E. Dumay, C.C. Valencia, J.L. Cuq, and J.L. Cheftel Surface hydrophobicity and aggregation of β-lactoglobulin heated near neutral pH J. Agric. Food Chem. 39 1994 2147 2155
17. E. Dufour, C. Genot, and T. Haertle β-Lactoglobulin binding properties during its 19 folding changes studied by fluorescence spectroscopy Biochim. Biophys. Acta 1205 1994 105 112
18. H. Katou, M. Hoshino, H. Kamikubo, C.A. Batt, and Y. Goto Native-like β-hairpin retained in the cold-denatured state of bovine β-lactoglobulin J. Mol. Biol. 310 2001 471 484
19. L.K. Creamer Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin Biochemistry 34 1995 7170 7176
20. D. Hamada, S. Segawa, and Y. Goto Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein Nat. Struct. Biol. 3 1996 868 873
21. V. Forge, M. Hoshino, K. Kuwata, M. Arai, K. Kuwajima, C.A. Batt, and Y. Goto Is folding of β-lactoglobulin non-hierarchic? Intermediate with native-like β-sheet and non-native alpha-helix J. Mol. Biol. 296 2000 1039 1051
22. D.R. Flower, A.C. North, and C.E. Sansom The lipocalin protein family: structural and sequence overview Biochim. Biophys. Acta 1482 2000 9 24
23. J.M. Armstrong, H.A. McKenzie, and W.H. Sawyer On the fractionation of β-lactoglobulin and α-lactalbumin Biochim. Biophys. Acta 147 1967 60 72
24. S. Kaminogawa, M. Hattori, O. Ando, J. Kurisaki, and K. Yamauchi Preparation of monoclonal antibody against bovine β-lactoglobulin and its unique affinity Agric. Biol. Chem. 51 1987 797 802
25. S. Futterman, and J. Heller The enhancement of fluorescence and decreased susceptibility to enzyme oxidation of retinol complexed with bovine serum albumin, β-lactoglobulin, and the retinol-binding protein of human plasma J. Biol. Chem. 247 1972 5168 5172
26. U. Cogan, M. Kopelman, S. Mokady, and M. Shintzky Binding affinities of retinol and related compounds to retinol binding proteins Eur. J. Biol. Chem. 65 1976 71 78
27. K. Weber, and M. Osborn The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis J. Biol. Chem. 244 1969 4406 4412
28. P.J. Hogg, S.C. Johnson, M.R. Bowles, S.M. Pond, and D.J. Winzor Evaluation of equilibrium constants for antigen-antibody interaction by solid-phase immunoassay: the binding of paraquat to its elicited mouse monoclonal antibody Mol. Immunol. 24 1987 797 801
29. T.P. Hopp, and K.R. Woods A computer program for predicting protein antigenic determinants Mol. Immunol. 20 1983 483 489
30. G.L. Ellman Tissue sulfhydryl groups Arch. Biochem. Biophys. 82 1959 70 77
31. J.S. Weissman, and P.S. Kim Reexamination of the folding of BPTI: predominance of native intermediates Science 253 1991 1386 1393
32. J.Y. Chang Identification of productive folding intermediates which account for the flow of protein folding pathway J. Biol. Chem. 268 1993 4043 4049
33. T.V. Burova, Y. Choiset, V. Tran, and T. Haertlé Role of free Cys121 in stabilization of bovine β-lactoglobulin B Protein Eng. 11 1998 1065 1073
34. M. Yagi, K. Sakurai, C. Kalidas, C.A. Batt, and Y. Goto Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group J. Biol. Chem. 278 2003 47009 47015
35. M. Hirose, T. Akuta, and N. Takahashi Renaturation of ovotransferrin under two-step conditions allowing primary folding of the fully reduced form and the subsequent regeneration of the intramolecular disulfides J. Biol. Chem. 264 1989 16867 16872