Pressure denaturation of β-lactoglobulin: Different stabilities of isoforms A and B, and an investigation of the Tanford transition

European Journal of Biochemistry

Volumn 267, Issue 8, 2000, Pages 2235-2241

  Botelho, Michelle M ^c   Valente Mesquita, Vera L ^c   Oliveira, Kesley M G ^a   Polikarpov, Igor ^a   Ferreira, Sérgio T ^b  

^a LABORATÓRIO NACIONAL DE LUZ SÍNCROTRON   (Brazil)

^b FEDERAL UNIVERSITY OF RIO DE JANEIRO   (Brazil)

^c NONE

Author keywords

lactoglobulin; Cavity; Hydrostatic pressure; Tanford transition; Thermodynamics

Indexed keywords

BETA LACTOGLOBULIN;

AMINO ACID SUBSTITUTION; ARTICLE; CATTLE; ENERGY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROSTATIC PRESSURE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; THERMODYNAMICS;

ANIMALS; CATTLE; GUANIDINE; HYDROGEN-ION CONCENTRATION; LACTOGLOBULINS; MODELS, MOLECULAR; PRESSURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN ISOFORMS; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

BOS TAURUS; BOVINAE;

EID: 0008845482     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.2000.01226.x     Document Type: Article

References (34)

1. 1. Weber, G. (1990) Whither biophysics? Annu. Rev. Biophys. Chem. 19, 1-6.
2. 2. Seibles, T.S. (1969) Interaction of dodecyl sulfate with native and modified beta-lactoglobulin. Biochemistry 8, 2949-2954.
3. 3. Spector, A.A. & Fletcher, J.E. (1970) Binding of long chain fatty acids to β-lactoglobulin. Lipids 5, 403-411.
4. 4. Fugate, R.D. & Song, P.-S. (1980) Spectroscopic characterization of β-lactoglobulin-retinol complex. Biochim. Biophys. Acta 625, 28-42.
5. 5. Pérez, M.D., Diaz de Villegas, M.C., Sanches, L., Aranda, P., Ena, J.M. & Calvo, M. (1989) Interaction of fatty acids with β-lactoglobulin and albumin from ruminant milk. Biochem. J. 106, 1094-1097.
6. 6. Narayan, M. & Berliner, L.J. (1997) Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochemistry 36, 1906-1911.
7. 7. Narayan, M. & Berliner, L.J. (1998) Mapping fatty acid binding to β-lactoglobulin: ligand binding is restricted by modification of Cys 121. Protein Sci. 7, 150-157.
8. 8. Lange, D.C., Kothari, R., Patel, R.C. & Patel, S.C. (1998) Retinol and retinoic acid bind to a surface cleft in bovine beta-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer. Biophys. Chem. 74, 45-51.
9. 9. Hambling, S.G., McAlpine, A.S. & Sawyer, L. (1992) β-Lactoglobulin. In Advanced Dairy Chemistry I (Fox, P.F., ed.), pp. 141-190. Elsevier, Amsterdam.
10. 10. Eigel, W., Butler, J.E., Ernstrom, C.A., Parrel, H.M. Jr, Harwalkar, V.R. & Whitney, R.M. (1984) Nomenclature of proteins of cow's milk: fifth revision. J. Dairy Sci. 67, 1599-1631.
11. 11. Godovac-Zimmermann, J., Conti, A., Sheil, M. & Napolitano, L. (1990) Covalent structure of the minor monomeric β-lactoglobulin II component from donkey milk. Biol. Chem. Hoppe-Seyler 371, 871-879.
12. 12. Godovac-Zimmermann, J., Krause, I., Baranyi, M., Fischer-Frühholz, S., Juszczak, J., Erhardt, G., Buchberger, J. & Klostermeyer, H. (1996) Isolation and rapid sequence characterization of two novel bovine β-lactoglobulin I and J. J. Protein Chem. 15, 743-750.
13. 13. Monaco, H.L., Zanotti, G., Spadon, P., Bolognesi, M., Sawyer, L. & Eliopoulos, E.E. (1987) Crystal structure of the trigonal form of bovine β-lactoglobulin and with retinol at 2.5 Å resolution. J. Mol. Biol. 197, 695-706.
14. 14. Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, H.M., Baker, E.N. & Jameson, G.B. (1998) Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry 37, 14014-14023.
15. 15. Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. & Jameson, G.B. (1999) Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Sci. 8, 75-83.
16. 16. Oliveira, K.M.G. (1999) High resolution X-ray fraction studies of bovine β-lactoglobulin. MSc Thesis, State University of Campinas, Brazil.
17. 17. Tanford, C., Bunville, L.G. & Nozaki, Y. (1959) The reversible transformation of β-lactoglobulin at pH 7.5. J. Am. Chem. Soc. 81, 4032-4036.
18. 18. Gross, M. & Jaenicke, R. (1994) Proteins under pressure. The influence of high hydrostatic pressure on structure, function and assembly of protein complexes. Eur. J. Biochem. 221, 617-630.
19. 19. Mozhaev, V.M., Heremans, K., Frank, J., Masson. P. & Balny, C. (1994) Exploiting the effects of hydrostatic pressure in biotechnological applications. Trends Biotechnol. 124, 494-501.
20. 20. Mozhaev, V.M., Heremans, K., Frank, J., Masson. P. & Balny, C. (1996) High pressure effects on protein structure and function. Proteins 24, 81-91.
21. 21. Dufour, E., Hui Bom Hoa, G. & Haertlé, T. (1994) High-pressure effects on β-lactoglobulin interactions with ligands studied by fluorescence. Biochim. Biophys. Acta 1206, 166-172.
22. 22. Funterberger, S., Dumay, E. & Cheftel, J.C. (1995) Pressure-induced aggregation of beta-lactoglobulin in pH 7 buffers. Food Sci. Technol. 28, 410-418.
23. 23. Funtenberger, S., Dumay, E. & Cheftel, J.C. (1997) High pressure promotes beta-lactoglobulin aggregation through SH/S-S interchange reactions. J. Agric. Food. Chem. 45, 912-921.
24. 24. Tanaka, N., Tsurui, Y., Kobayashi, I. & Kunugi, S. (1996) Modification of the single unpaired sulfhydril group of beta-lactoglobulin under high pressure and the role of intermolecular S-S exchange in the pressure denaturation. Int. J. Biol. Macromol. 19, 63-68.
25. 25. Valente-Mesquita, V.L., Botelho, M.M. & Ferreira, S.T. (1998) Pressure-induced subunit dissociation and unfolding of β-lactoglobulin. Biophys. J. 75, 471-476.
26. 26. Paladini, A. Jr & Weber, G. (1981) Pressure-induced reversible dissociation of enolase. Biochemistry 20, 2587-2593.
27. 27. Weber, G. (1987) Dissociation of oligomeric proteins by hydrostatic pressure. In High Pressure Chemistry and Biochemistry (van Eldyk, R. & Jonas, J., eds), ASI Series 197, pp. 401-420, NATO.
28. 28. Panick, G., Malessa, R. & Winter, R. (1999) Differences between the pressure-and temperature-induced denaturation and aggregation of β-lactoglobulin A, B and AB monitored by FTIR spectroscopy and small-angle X-ray scattering. Biochemistry 38, 6512-6519.
29. 29. Matthews, B.W. (1993) Structural and genetic analysis of protein stability. Annu. Rev. Biochem. 62, 139-160.
30. 30. Eriksson, A.E., Baase, W.A., Zhang, X.J., Heinz, D.W., Blaber, M., Baldwin, E. & Matthews, B.W. (1992) Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. Science 255, 178-183.
31. 31. Consonni, R., Santomo, L., Fusi, P., Tortora, P. & Zetta, L. (1999) A single point mutation in the extreme heat-and pressure-resistant Sso7d protein from Sulfolobus solfataricus leads to a major rearrangement of the hydrophobic core. Biochemistry 38, 12709-12717.
32. 32. Shortle, D., Stiles, W.E. & Meeker, A.K. (1990) Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry 29, 8033-8041.
33. 33. Dong, A., Matsuura, J., Allison, S.D., Chrisman, E., Manning, M.C. & Carpenter, J.F. (1996) Infrared and circular dichroism spectroscopic characterization of structural differences between β-lactoglobulin A and B. Biochemistry 35, 1450-1457.
34. 34. Pedersen, K.O. (1936) Ultracentrifugal and electrophoretic studies on the milk proteins. II. The lactoglobulins of Palmer. Biochem. J. 30, 961-970.