Structure and Stability of Whey Proteins

Milk Proteins

Volumn , Issue , 2008, Pages 163-203

  Edwards, Patrick B ^a   Creamer, Lawrence K ^a   Jameson, Geoffrey B ^a  

^a MASSEY UNIVERSITY   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 76749104459     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374039-7.00006-4     Document Type: Chapter

References (202)

1. Acharya K.R., Stuart D.I., Walker N.P.C., Lewis M., Phillips D.C. Refined structure of baboon α-lactalbumin at 1.7 Å resolution. Comparison with C type lysozyme. Journal of Molecular Biology 1989, 208:99-127.
2. Acharya K.R., Ren J.S., Stuart D.I., Phillips D.C., Fenna R.E. Crystal structure of human α-lactalbumin at 1.7 Å resolution. Journal of Molecular Biology 1991, 221:571-581.
3. Adams J.J., Anderson B.F., Norris G.E., Creamer L.K., Jameson G.B. Structure of bovine β-lactoglobulin (variant A) at very low ionic strength. Journal of Structural Biology 2006, 154:246-254.
4. Ahmad N., Qasim M.A. Fatty acid binding to bovine serum albumin prevents formation of intermediate during denaturation. European Journal of Biochemistry 1995, 227:563-565.
5. Ahmad B., Ahmed Md Z., Haq S.K., Khan R.H. Guanidine hydrochloride denaturation of human serum albumin originates by local unfolding of some stable loops in domain III. Biochimica et Biophysica Acta 2005, 1750:93-102.
6. Alexander S.S., Pace C.N. A comparison of the denaturation of bovine β-lactoglobulins A and B and goat β-lactoglobulin. Biochemistry 1971, 10:2738-2743.
7. Anderson B.F., Baker H.M., Dodson E.J., Norris G.E., Rumball S.V., Waters J.M., Baker E.N. Structure of human lactoferrin at 3.2 Å resolution. Proceedings of the National Academy of Sciences of the United States of America 1987, 84:1769-1773.
8. Anderson B.F., Baker H.M., Norris G.E., Rice D.W., Baker E.N. Structure of human lactoferrin - crystallographic structure-analysis and refinement at 2.8 Å resolution. Journal of Molecular Biology 1989, 209:711-734.
9. Aouzelleg A., Bull L.-A., Price N.C., Kelly S.M. Molecular studies of pressure/temperature-induced structural changes in bovine β-lactoglobulin. Journal of the Science of Food and Agriculture 2004, 84:398-404.
10. Baker H.M., Baker E.N. Lactoferrin and iron: structural and dynamic aspects of binding and release. BioMetals 2004, 17:209-216.
11. Banaszak L., Winter N., Xu Z., Bernlohr D.A., Cowan S., Jones T.A. Lipid-binding proteins: a family of fatty acid and retinoid transport proteins. Advances in Protein Chemistry 1994, 45:89-151.
12. 1H NMR study. Journal of Agricultural and Food Chemistry 1998, 46:1805-1813.
13. 1H-NMR study on the effect of high pressures on β-lactoglobulin. Journal of Agricultural and Food Chemistry 2000, 48:3906-3912.
14. Bennion B.J., Daggett V. The molecular basis for the chemical denaturation of proteins by urea. Proceedings of the National Academy of Sciences of the United States of America 2003, 100:5142-5147.
15. Bewley, M. C., Qin, B. Y., Jameson, G. B., Sawyer, L., and Baker, E. N. (1997). Bovine β-lactoglobulin and its variants: a three-dimensional structural perspective. In: Milk Protein Polymorphism, IDF Special Issue 9702, pp. 100-9. Brussels: International Dairy Federation.
16. Bhattacharjee C., Saha S., Biswas A., Kundu M., Ghosh L., Das K.P. Structural changes of β-lactoglobulin during thermal unfolding and refolding-an FT-IR and circular dichroism study. Protein Journal 2005, 24:27-35.
17. Bhattacharya A.A., Curry S., Franks N.P. Binding of the general anesthetics propofol and halothane to human serum albumin - high resolution crystal structures. Journal of Biological Chemistry 2000, 275:38731-38738.
18. Brew, K. (2003). α-Lactalbumin. In: Advanced Dairy Chemistry, Volume 1, Proteins, 3rd edn. (P. F. Fox and P. L. H. McSweeney, eds) pp. 387-419. New York: Kluwer Academic/Plenum Publishers.
19. Brock J.H. The physiology of lactoferrin. Biochemistry and Cell Biology 2002, 80:1-6.
20. Brownlow S., Cabral J.H.M., Cooper R., Flower D.R., Yewdall S.J., Polikarpov I., North A.C., Sawyer L. Bovine β-lactoglobulin at 1.8 Å resolution - still an enigmatic lipocalin. Structure (London) 1997, 5:481-495.
21. Burova T.V., Grinberg N.V., Visschers R.W., Grinberg V.Y., de Kruif C.G. Thermodynamic stability of porcine β-lactoglobulin-a structural relevance. European Journal of Biochemistry 2002, 269:3958-3968.
22. Busti P., Gatti C.A., Delorenzi N.J. Binding of alkylsulfonate ligands to bovine β-lactoglobulin: effects on protein thermal unfolding. Food Research International 2006, 39:503-509.
23. Calderone V., Giuffrida M.G., Viterbo D., Napolitano L., Fortunato D., Conti A., Acharya K.R. Amino acid sequence and crystal structure of buffalo α-lactalbumin. FEBS Letters 1996, 394:91-95.
24. Carballal S., Alvarez B., Turell L., Botti H., Freeman B.A., Radi R. Sulfenic acid in human serum albumin. Amino Acids 2007, 32:543-551.
25. Casal H.L., Kohler U., Mantsch H.H. Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature. Biochimica et Biophysica Acta 1988, 957:11-20.
26. Cavanagh J., Fairbrother W., Palmer A.G., Skelton N. Protein NMR Spectroscopy: Principles and Practice 1995, Academic Press, San Diego, California.
27. Chamani J., Moosavi-Movahedi A.A., Rajabi O., Gharanfoli M., Momen-Heravi M., Hakimelahi G.H., Neamati-Baghsiah A., Varasteh A.R. Cooperative α-helix formation of β-lactoglobulin induced by sodium n-alkyl sulfates. Journal of Colloid and Interface Science 2006, 293:52-60.
28. Chandra N., Brew K., Acharya K.R. Structural evidence for the presence of a secondary calcium binding site in human α-lactalbumin. Biochemistry 1998, 37:4767-4772.
29. Chatterton D.E.W., Smithers G., Roupas P., Brodkorb A. Bioactivity of β-lactoglobulin and α-lactalbumin - technological implications for processing. International Dairy Journal 2006, 16:1229-1240.
30. Chaudhuri T.K., Horii K., Yoda T., Arai M., Nagata S., Terada T.P., Uchiyama H., Ikura T., Tsumoto K., Kataoka H., Matsushima M., Kuwajima K., Kumagai I. Effect of the extra N-terminal methionine residue on the stability and folding of recombinant α-lactalbumin expressed in Escherichia coli. Journal of Molecular Biology 1999, 285:1179-1194.
31. Cho Y., Gu W., Watkins S., Lee S.P., Kim T.R., Brady J.W., Batt C.A. Thermostable variants of bovine β-lactoglobulin. Protein Engineering 1994, 7:263-270.
32. Chrysina E.D., Brew K., Acharya K.R. Crystal structures of apo- and holo-bovine α-lactalbumin at 2.2 Å resolution reveal an effect of calcium on inter-lobe interactions. Journal of Biological Chemistry 2000, 275:37021-37029.
33. Cistola D.P., Small D.M., Hamilton J.A. Carbon 13 NMR studies of saturated fatty acids bound to bovine serum albumin. 1. The filling of individual fatty-acid binding sites. Journal of Biological Chemistry 1987, 262:10971-10979.
34. 15N nuclear magnetic relaxation of proteins. Journal of the American Chemical Society 1990, 112:4989-4991.
35. Considine T., Patel H.A., Singh H., Creamer L.K. Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalene-sulfonate on the heat-induced unfolding and aggregation of β-lactoglobulin B. Journal of Agricultural and Food Chemistry 2005, 53:3197-3205.
36. Considine T., Singh H., Patel H.A., Creamer L.K. Influence of binding of sodium dodecyl sulfate, all-trans-retinol, and 8-anilino-1-naphthalenesulfonate on the high-pressure-induced unfolding and aggregation of β-lactoglobulin B. Journal of Agricultural and Food Chemistry 2005, 53:8010-8018.
37. Cornish J., Callon K.E., Naot D., Palmano K.P., Banovic T., Bava U., Watson M., Lin J.-M., Tong P.C., Chen Q., Chan V.A., Reid H.E., Fazzalari N., Baker H.M., Baker E.N., Haggarty N.W., Grey A.B., Reid I.R. Lactoferrin is a potent regulator of bone cell activity and increases bone formation in vivo. Endocrinology 2004, 145:4366-4374.
38. Creamer L.K. Effect of sodium dodecyl sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry 1995, 34:7170-7176.
39. S1- and β-casein in solution. Archives of Biochemistry and Biophysics 1981, 211:689-696.
40. Creamer L.K., Parry D.A.D., Malcolm G.N. Secondary structure of bovine β-lactoglobulin B. Archives of Biochemistry and Biophysics 1983, 227:98-105.
41. Creamer L.K., Blair M., Korte R., Jameson G.B. Binding of small amphipathic molecules to β-lactoglobulin. Journal of Dairy Science 2000, 83(Suppl.1):99. Abstract 424.
42. Creamer L.K., Bienvenue A., Nilsson H., Paulsson M., Van Wanroij M., Lowe E.K., Anema S.G., Boland M.J., Jimenez-Flores R. Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine β-lactoglobulin. Journal of Agricultural and Food Chemistry 2004, 52:7660-7668.
43. Cupp D., Kampf J.P., Kleinfeld A.M. Fatty acid-albumin complexes and the determination of the transport of long chain free fatty acids across membranes. Biochemistry 2004, 43:4473-4481.
44. Curry S., Mandelkow H., Brick P., Franks N. Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nature Structural Biology 1998, 5:827-835.
45. D'Alfonso L., Collini M., Baldini G. Does β-lactoglobulin denaturation occur via an intermediate state?. Biochemistry 2002, 41:326-333.
46. D'Alfonso L., Collini M., Ragona L., Ugolini R., Baldini G., Molinari H. Porcine β-lactoglobulin chemical unfolding: identification of a non-native α-helical intermediate. Proteins: Structure Function and Bioinformatics 2004, 58:70-79.
47. Dar T.A., Singh L.R., Islam A., Anjum F., Moosavi-Movahedi A.A., Ahmad F. Guanidinium chloride and urea denaturations of β-lactoglobulin A at pH 2.0 and 25°C: the equilibrium intermediate contains non-native structures (helix, tryptophan and hydrophobic patches). Biophysical Chemistry 2007, 127:140-148.
48. de Laureto P.P., Frare E., Gottardo R., Fontana A. Molten globule of bovine α-lactalbumin at neutral pH induced by heat, trifluoroethanol, and oleic acid: a comparative analysis by circular dichroism spectroscopy and limited proteolysis. Proteins: Structure Function and Genetics 2002, 49:385-397.
49. de Wit J.N., Swinkels G.A.M. A differential scanning calorimetric study of the thermal denaturation of bovine β-lactoglobulin. Thermal behavior at temperatures up to 100°C. Biochimica et Biophysica Acta, Protein Structure 1980, 624:40-50.
50. Delano W.L. PyMOL 2002, Delano Scientific, Palo Alto, California.
51. Denton H., Smith M., Husi H., Uhrín D., Barlow P.N., Batt C.A., Sawyer L. Isotopically labeled bovine β-lactoglobulin for NMR studies expressed in Pichia pastoris. Protein Expression and Purification 1998, 14:97-103.
52. Dolgikh D.A., Gilmanshin R.I., Brazhnikov E.V., Bychkova V.E., Semisotnov G.V., Venyaminov S.Y., Ptitsyn O.B. α-Lactalbumin: compact state with fluctuating tertiary structure?. FEBS Letters 1981, 136:311-315.
53. Dufour E., Genot C., Haertlé T. β-Lactoglobulin binding properties during its folding changes studied by fluorescence spectroscopy. Biochimica et Biophysica Acta 1994, 1205:105-112.
54. Dufour E., Hervé G., Haertlé T. Hydrolysis of β-lactoglobulin by thermolysin and pepsin under high hydrostatic pressure. Biopolymers 1995, 35:475-483.
55. Dzwolak W., Kato M., Shimizu A., Taniguchi Y. Fourier-transform infrared spectroscopy study of the pressure-induced changes in the structure of the bovine α-lactalbumin: the stabilizing role of the calcium ion. Biochimica et Biophysica Acta Protein Structure and Molecular Enzymology 1999, 1433:45-55.
56. Edwards P.J.B., Jameson G.B., Palmano K.P., Creamer L.K. Heat-resistant structural features of bovine β-lactoglobulin A revealed by NMR H/D exchange observations. International Dairy Journal 2002, 12:331-344.
57. Edwards, P. J. B., Uhrín, D., Jameson, G. B., Loo, T., Norris, G. E. and Barlow, P. N. (2003). Backbone dynamics of bovine β-lactoglobulin from 15N NMR measurements. Unpublished results.
58. Farrell H.M., Jimenez-Flores R., Bleck G.T., Brown E.M., Butler J.E., Creamer L.K., Hicks C.L., Hollar C.M., Ng-Kwai-Hang K.F., Swaisgood H.E. Nomenclature of the proteins of cows' milk - sixth revision. Journal of Dairy Science 2004, 87:1641-1674.
59. Farruggia B., Nerli B., Di Nuci H., Rigatusso R., Pico G. Thermal features of the bovine serum albumin unfolding by polyethylene glycols. International Journal of Biological Macromolecules 1999, 26:23-33.
60. Fast J., Mossberg A.-K., Svanborg C., Linse S. Stability of HAMLET-a kinetically trapped α-lactalbumin oleic acid complex. Protein Science 2005, 14:329-340.
61. Flower D.R. The lipocalin protein family: structure and function. Biochemical Journal 1996, 318:1-14.
62. Fogolari F., Ragona L., Zetta L., Romagnoli S., de Kruif K.G., Molinari H. Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Letters 1998, 436:149-154.
63. Frapin D., Dufour E., Haertlé T. Probing the fatty acid binding site of β-lactoglobulins. Journal of Protein Chemistry 1993, 12:443-449.
64. Gapper L., Copestake D., Otter D., Indyk H. Analysis of bovine immunoglobulin G in milk, colostrum and dietary supplements: a review. Analytical and Bioanalytical Chemistry 2007, 389:93-109.
65. Ghuman J., Zunszain P.A., Petitpas I., Bhattacharya A.A., Otagiri M., Curry S. Structural basis of the drug-binding specificity of human serum albumin. Journal of Molecular Biology 2005, 353:38-52.
66. Glasgow B.J., Abduragimov A.R., Farahbakhsh Z.T., Faull K.F., Hubbell W.L. Tear lipocalins bind a broad array of lipid ligands. Current Eye Research 1995, 14:363-372.
67. Gosal W.S., Clark A.H., Pudney P.D.A., Ross-Murphy S.B. Novel amyloid fibrillar networks derived from a globular protein: β-lactoglobulin. Langmuir 2002, 18:7174-7181.
68. Gottschalk M., Nilsson H., Roos H., Halle B. Protein self-association in solution: the bovine β-lactoglobulin dimer and octamer. Protein Science 2003, 12:2404-2411.
69. Green D.W., Aschaffenburg R., Camerman A., Coppola J.C., Dunnill P., Simmons R.M., Komorowski E.S., Sawyer L., Turner E.M.C., Woods K.F. Structure of bovine β-lactoglobulin at 6 Å resolution. Journal of Molecular Biology 1979, 131:375-397.
70. Grobler J.A., Rao K.R., Pervaiz S., Brew K. Sequences of two highly divergent canine type c lysozymes: implications for the evolutionary origins of the lysozyme/α-lactalbumin superfamily. Archives of Biochemistry and Biophysics 1994, 313:360-366.
71. Groves M.L., Hipp N.J., McMeekin T.L. Effect of pH on the denaturation of β-lactoglobulin and its dodecyl sulfate derivative. Journal of the American Chemical Society 1951, 73:2790-2793.
72. Guo L.-H., Qu N. Chemical-induced unfolding of cofactor-free protein monitored by electrochemistry. Analytical Chemistry 2006, 78:6275-6278.
73. Guss J.M., Messer M., Costello M., Hardy K., Kumar V. Structure of the calcium-binding echidna milk lysozyme at 1.9 Å resolution. Acta Crystallographica, Section D: Biological Crystallography 1997, D53:355-363.
74. Ha E., Zemel M.B. Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people. Journal of Nutritional Biochemistry 2003, 14:251-258.
75. Hagihara Y., Aimoto S., Fink A.L., Goto Y. Guanidine hydrochloride-induced folding of proteins. Journal of Molecular Biology 1993, 231:180-184.
76. Hamada D., Goto Y. The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure. Journal of Molecular Biology 1997, 269:479-487.
77. Hamada D., Kuroda Y., Tanaka T., Goto Y. High helical propensity of the peptide fragments derived from β-lactoglobulin, a predominantly β-sheet protein. Journal of Molecular Biology 1995, 254:737-746.
78. Hambling, S. G., McAlpine, A. S. and Sawyer, L. (1992). β-Lactoglobulin. In: Advanced Dairy Chemistry, Volume 1, Proteins, 2nd edn (P. F. Fox, ed.) pp. 141-90. Barking, Essex: Elsevier Applied Science.
79. 13C NMR study. Proceedings of the National Academy of Sciences of the United States of America- Biological Sciences 1984, 81:3718-3722.
80. Hamilton J.A., Era S., Bhamidipati S.P., Reed R.G. Locations of the 3 primary binding sites for long-chain fatty acids on bovine serum albumin. Proceedings of the National Academy of Sciences of the United States of America 1991, 88:2051-2054.
81. Haridas M., Anderson B.F., Baker E.N. Structure of human diferric lactoferrin refined at 2.2 Å resolution. Acta Crystallographica Section D: Biological Crystallography 1995, 51:629-646.
82. Havea P., Singh H., Creamer L.K. Characterization of heat-induced aggregates of β-lactoglobulin, α-lactalbumin and bovine serum albumin in a whey protein concentrate environment. Journal of Dairy Research 2001, 68:483-497.
83. Ho J.X., Holowachuk E.W., Norton E.J., Twigg P.D., Carter D.C. X-ray and primary structure of horse serum-albumin (Equus-caballus) at 0.27nm resolution. European Journal of Biochemistry 1993, 215:205-212.
84. Hoedemaeker F.J., Visschers R.W., Alting A.C., de Kruif K.G., Kuil M.E., Abrahams J.P. A novel pH-dependent dimerization motif in β-lactoglobulin from pig (Sus scrofa). Acta Crystallographica Section D: Biological Crystallography 2002, D58:480-486.
85. Hong Y.-H., Creamer L.K. Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment. International Dairy Journal 2002, 12:345-359.
86. Iametti S., De Gregori B., Vecchio G., Bonomi F. Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. European Journal of Biochemistry 1996, 237:106-112.
87. Iametti S., Transidico P., Bonomi F., Vecchio G., Pittia P., Rovere P., Dall'Aglio G. Molecular modifications of β-lactoglobulin upon exposure to high pressure. Journal of Agricultural and Food Chemistry 1997, 45:23-29.
88. Invernizzi G., Samalikova M., Brocca S., Lotti M., Molinari H., Grandori R. Comparison of bovine and porcine β-lactoglobulin: a mass spectrometric analysis. Journal of Mass Spectrometry 2006, 41:717-727.
89. Ishikawa N., Chiba T., Chen L.T., Shimizu A., Ikeguchi M., Sugai S. Remarkable destabilization of recombinant α-lactalbumin by an extraneous N-terminal methionyl residue. Protein Engineering 1998, 11:333-335.
90. Jameson G.B., Anderson B.F., Norris G.E., Thomas D.H., Baker E.N. Structure of human apolactoferrin at 2.0 Å resolution. Refinement and analysis of ligand-induced conformational change. Acta Crystallographica, Section D: Biological Crystallography 1998, 54:1319-1335.
91. Jameson G.B., Anderson B.F., Norris G.E., Thomas D.H., Baker E.N. Structure of human apolactoferrin at 2.0 Å resolution. Refinement and analysis of ligand-induced conformational change (corrigendum 54:1319). Acta Crystallographica, Section D: Biological Crystallography 1999, 55:1108.
92. Jameson G.B., Adams J.J., Creamer L.K. Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin. International Dairy Journal 2002, 12:319-329.
93. Jameson G.B., Anderson B.F., Breyer W.A., Day C.L., Tweedie J.W., Baker E.N. Structure of a domain-opened mutant (R121D) of the human lacto-ferrin N-lobe refined from a merohedrally twinned crystal form. Acta Crystallographica, Section D: Biological Crystallography 2002, 58:955-962.
94. Jegouic M., Grinberg V.Y., Guingant A., Haertlé T. Thiol-induced oligo-merization of α-lactalbumin at high pressure. Journal of Protein Chemistry 1996, 15:501-509.
95. Kaminogawa S., Shimizu M., Ametani A., Hattori M., Ando O., Hachimura S., Nakamura Y., Totsuka M., Yamauchi K. Monoclonal antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin. Biochimica et Biophysica Acta 1989, 998:50-56.
96. Karthikeyan S., Paramasivam M., Yadav S., Srinivasan A., Singh T.P. Structure of buffalo lactoferrin at 2.5 Å resolution using crystals grown at 303K shows different orientations of the N and C lobes. Acta Crystallographica Section D: Biological Crystallography 1999, 55:1805-1813.
97. Kawakami A., Kubota K., Yamada N., Tagami U., Takehana K., Sonaka I., Suzuki E., Hirayama K. Identification and characterization of oxidized human serum albumin. A slight structural change impairs its ligand-binding and antioxidant functions. FEBS Journal 2006, 273:3346-3357.
98. Kella N.K., Kinsella J.E. Enhanced thermodynamic stability of β-lactoglobulin at low pH. A possible mechanism. Biochemical Journal 1988, 255:113-118.
99. Khan M.Y., Agarwal S.K., Hangloo S. Urea-induced structural transformations in bovine serum albumin. Journal of Biochemistry (Tokyo, Japan) 1987, 102:313-317.
100. Kim T.-R., Goto Y., Hirota N., Kuwata K., Denton H., Wu S.-Y., Sawyer L., Batt C.A. High-level expression of bovine β-lactoglobulin in Pichia pastoris and characterization of its physical properties. Protein Engineering 1997, 10:1339-1345.
101. Knudsen J.C., Otte J., Olsen K., Skibsted L.H. Effect of high hydrostatic pressure on the conformation of β-lactoglobulin A as assessed by proteolytic peptide profiling. International Dairy Journal 2002, 12:791-803.
102. Kobayashi T., Ikeguchi M., Sugai S. Molten globule structure of equine β-lactoglobulin probed by hydrogen exchange. Journal of Molecular Biology 2000, 299:757-770.
103. Kobayashi T., Ikeguchi M., Sugai S. Construction and characterization of β-lactoglobulin chimeras. Proteins: Structure Function and Genetics 2002, 49:297-301.
104. Kontopidis G., Holt C., Sawyer L. β-Lactoglobulin: binding properties, structure, and function. Journal of Dairy Science 2004, 87:785-796.
105. Konuma T., Sakurai K., Goto Y. Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity. Journal of Molecular Biology 2007, 368:209-218.
106. 19F magnetic relaxation dispersion. Biochemistry 2003, 42:13708-13716.
107. Kumar Y., Muzammil S., Tayyab S. Influence of fluoro, chloro and alkyl alcohols on the folding pathway of human serum albumin. Journal of Biochemistry (Tokyo, Japan) 2005, 138:335-341.
108. Kumosinski T.F., Timasheff S.N. Molecular interactions in β-lactoglobulin. X. The stoichiometry of the β-lactoglobulin mixed tetramerization. Journal of the American Chemical Society 1966, 88:5635-5642.
109. Kuroda Y., Hamada D., Tanaka T., Goto Y. High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy. Folding and Design 1996, 1:255-263.
110. Kuwajima K. The molten globule state of α-lactalbumin. FASEB Journal 1996, 10:102-109.
111. Kuwata K., Hoshino M., Era S., Batt C.A., Goto Y. α→β transition of β-lactoglobulin as evidenced by heteronuclear NMR. Journal of Molecular Biology 1998, 283:731-739.
112. Kuwata K., Hoshino M., Forge V., Era S., Batt C.A., Goto Y. Solution structure and dynamics of bovine β-lactoglobulin A. Protein Science 1999, 8:2541-2545.
113. Kuwata K., Li H., Yamada H., Batt C.A., Goto Y., Akasaka K. High pressure NMR reveals a variety of fluctuating conformers in β-lactoglobulin. Journal of Molecular Biology 2001, 305:1073-1083.
114. Lampreave F., Piñeiro A., Brock J.H., Castillo H., Sánchez L., Calvo M. Interaction of bovine lactoferrin with other proteins of milk whey. International Journal of Biological Macromolecules 1990, 12:2-5.
115. Lange D.C., Kothari R., Patel R.C., Patel S.C. Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer. Biophysical Chemistry 1998, 74:45-51.
116. Lapanje S., Skerjanc J. Dilatometric study of the denaturation of bovine serum albumin by guanidine hydrochloride. Biochemical and Biophysical Research Communications 1974, 56:338-342.
117. Li S.Q., Bomser J.A., Zhang Q.H. Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G. Journal of Agricultural and Food Chemistry 2005, 53:663-670.
118. Lipari G., Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. Journal of the American Chemical Society 1982, 104:4546-4559.
119. Lopez-Fandino R. Functional improvement of milk whey proteins induced by high hydrostatic pressure. Critical Reviews in Food Science and Nutrition 2006, 46:351-363.
120. Lopez-Fandino R. High pressure-induced changes in milk proteins and possible applications in dairy technology. International Dairy Journal 2006, 16:1119-1131.
121. Luebke M., Guichard E., Tromelin A., Le Quere J.L. Nuclear magnetic resonance spectroscopic study of β-lactoglobulin interactions with two flavor compounds, γ-decalactone and β-ionone. Journal of Agricultural and Food Chemistry 2002, 50:7094-7099.
122. Mainer G., Sanchez L., Ena J.M., Calvo M. Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA and IgM. Journal of Food Science 1997, 62:1034-1038.
123. Manderson, G.A., Hardman, M.J., and Creamer, L.K. (1997). Spectroscopic examination of the heat-induced changes in β-lactoglobulin A, B and C. In Milk Protein Polymorphism, IDF Special Issue 9702, pp. 204-211. Brussels: International Dairy Federation.
124. McGuffey M.K., Epting K.L., Kelly R.M., Foegeding E.A. Denaturation and aggregation of three α-lactalbumin preparations at neutral pH. Journal of Agricultural and Food Chemistry 2005, 53:3182-3190.
125. McKenzie H.A., Sawyer W.H. Effect of pH on β-lactoglobulins. Nature (London) 1967, 214:1101-1104.
126. Messens W., Van Camp J., Dewettinck K. High-pressure processing to improve dairy product quality. Dairy Processing: Improving Quality 2003, 310-332. CRC Press LLC, Boca Raton, Florida.
127. Mills O.E. Effect of temperature on tryptophan fluorescence of β-lactoglobulin B. Biochimica et Biophysica Acta 1976, 434:324-332.
128. Moller R.E., Stapelfeldt H., Skibsted L.H. Thiol reactivity in pressure-unfolded β-lactoglobulin. Antioxidative properties and thermal refolding. Journal of Agricultural and Food Chemistry 1998, 46:425-430.
129. Monaco H.L., Zanotti G., Spadon P., Bolognesi M., Sawyer L., Eliopoulos E.E. Crystal structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution. Journal of Molecular Biology 1987, 197:695-706.
130. Moore S.A., Anderson B.F., Groom C.R., Haridas M., Baker E.N. Three-dimensional structure of diferric bovine lactoferrin at 2.8 Å resolution. Journal of Molecular Biology 1997, 274:222-236.
131. Musante L., Bruschi M., Candiano G., Petretto A., Dimasi N., Del Boccio P., Urbani A., Rialdi G., Ghiggeri G.M. Characterization of oxidation end product of plasma albumin 'in vivo'. Biochemical and Biophysical Research Communications 2006, 349:668-673.
132. Muzammil S., Kumar Y., Tayyab S. Anion-induced stabilization of human serum albumin prevents the formation of intermediate during urea denaturation. Proteins: Structure Function and Genetics 2000, 40:29-38.
133. Narayan M., Berliner L.J. Mapping fatty acid binding to β-lactoglobulin: ligand binding is restricted by modification of Cys 121. Protein Science 1998, 7:150-157.
134. Nishikawa K., Noguchi T. Predicting protein secondary structure based on amino acid sequence. Methods in Enzymology 1991, 202:31-44.
135. Oksanen E., Jaakola V.P., Tolonen T., Valkonen K., Aakerstroem B., Kalkkinen N., Virtanen V., Goldman A. Reindeer β-lactoglobulin crystal structure with pseudo-body-centered noncrystallographic symmetry. Acta Crystallographica Section D: Biological Crystallography 2006, D62:1369-1374.
136. Okuno A., Kato M., Taniguchi Y. Pressure effects on the heat-induced aggregation of equine serum albumin by FT-IR spectroscopic study: secondary structure, kinetic and thermodynamic properties. Biochimica et Biophysica Acta Proteins and Proteomics 2007, 1774:652-660.
137. Oria R., Ismail M., Sánchez L., Calvo M., Brock J.H. Effect of heat treatment and other milk proteins on the interaction of lactoferrin with monocytes. Journal of Dairy Research 1993, 60:363-369.
138. Pace C.N., Tanford C. Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55°. Biochemistry 1968, 7:198-208.
139. Panick G., Malessa R., Winter R. Differences between the pressure and temperature induced denaturation and aggregation of β-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle x-ray scattering. Biochemistry 1999, 38:6512-6519.
140. Papiz M.Z., Sawyer L., Eliopoulos E.E., North A.C.T., Findlay J.B.C., Sivaprasadarao R., Jones T.A., Newcomer M.E., Kraulis P.J. The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature (London) 1986, 324:383-385.
141. Patel H.A., Singh H., Havea P., Considine T., Creamer L.K. Pressure-induced unfolding and aggregation of the proteins in whey protein concentrate solutions. Journal of Agricultural and Food Chemistry 2005, 53:9590-9601.
142. Pedersen K.O. Ultracentrifugal and electrophoretic studies on the milk proteins: the lactoglobulin of Palmer. Biochemical Journal 1936, 30:961-970.
143. Permyakov E.A., Berliner L.J. α-Lactalbumin: structure and function. FEBS Letters 2000, 473:269-274.
144. Pike A.C.W., Brew K., Acharya K.R. Crystal structures of guinea pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase. Structure (London) 1996, 4:691-703.
145. Puyol P., Perez M.D., Peiro J.M., Calvo M. Effect of binding of retinol and palmitic acid to bovine β-lactoglobulin on its resistance to thermal denaturation. Journal of Dairy Science 1994, 77:1402-1494.
146. Qi X.L., Brownlow S., Holt C., Sellers P. Thermal denaturation of β-lactoglobulin: effect of protein concentration at pH 6.75 and 8.05. Biochimica et Biophysica Acta 1995, 1248:43-49.
147. Qi X.L., Holt C., McNulty D., Clarke D.T., Brownlow S., Jones G.R. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: a test of the molten globule hypothesis. Biochemical Journal 1997, 324:341-346.
148. Qin B.Y., Bewley M.C., Creamer L.K., Baker H.M., Baker E.N., Jameson G.B. Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry 1998, 37:14014-14023.
149. Qin B.Y., Creamer L.K., Baker E.N., Jameson G.B. 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Letters 1998, 438:272-278.
150. Qin B.Y., Bewley M.C., Creamer L.K., Baker E.N., Jameson G.B. Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Science 1999, 8:75-83.
151. Ragona L., Pusterla F., Zetta L., Monaco H.L., Molinari H. Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Folding and Design 1997, 2:281-290.
152. Ragona L., Fogolari F., Romagnoli S., Zetta L., Maubois J.L., Molinari H. Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements. Journal of Molecular Biology 1999, 293:953-969.
153. Ragona L., Fogolari F., Zetta L., Perez D.M., Puyol P., de Kruif K.G., Lohr F., Ruterjans H., Molinari H. Bovine β-lactoglobulin: interaction studies with palmitic acid. Protein Science 2000, 9:1347-1356.
154. Ragona L., Fogolari F., Catalano M., Ugolini R., Zetta L., Molinari H. EF loop conformational change triggers ligand binding in β-lactoglobulins. Journal of Biological Chemistry 2003, 278:38840-38846.
155. Relkin P. Thermal unfolding of β-lactoglobulin, α-lactalbumin, and bovine serum albumin. A thermodynamic approach. Critical Reviews in Food Science and Nutrition 1996, 36:565-601.
156. Relkin P., Eynard L., Launay B. Thermodynamic parameters of β-lactoglobulin and α-lactalbumin. A DSC study of denaturation by heating. Thermochimica Acta 1992, 204:111-121.
157. 2+ binding to bovine lactoferrin enhances protein stability and influences the release of bacterial lipopolysaccharide. Biochemistry and Cell Biology 2002, 80:41-48.
158. Ruegg M., Moor U., Blanc B. Calorimetric study of thermal-denaturation of whey proteins in simulated milk ultrafiltrate. Journal of Dairy Research 1977, 44:509-520.
159. Sakai K., Sakurai K., Sakai M., Hoshino M., Goto Y. Conformation and stability of thiol-modified bovine β-lactoglobulin. Protein Science 2000, 9:1719-1729.
160. Sakurai K., Goto Y. Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution. Journal of Biological Chemistry 2002, 277:25735-25740.
161. Sakurai K., Goto Y. Dynamics and mechanism of the Tanford transition of bovine β-lactoglobulin studied using heteronuclear NMR spectroscopy. Journal of Molecular Biology 2006, 356:483-496.
162. Sakurai K., Oobatake M., Goto Y. Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3. Protein Science 2001, 10:2325-2335.
163. Sakurai Y., Ma S.F., Watanabe H., Yamaotsu N., Hirono S., Kurono Y., Kragh-Hansen U., Otagiri M. Esterase-like activity of serum albumin: characterization of its structural chemistry using p-nitrophenyl esters as substrates. Pharmaceutical Research 2004, 21:285-292.
164. Sánchez L., Peiró J.M., Castillo H., Pérez M.D., Ena J.M., Calvo M. Kinetic parameters for denaturation of bovine milk lactoferrin. Journal of Food Science 1992, 57:873-879.
165. Sawyer L., Brownlow S., Polikarpov I., Wu S.-Y. β-Lactoglobulin: structural studies, biological clues. International Dairy Journal 1998, 8:65-72.
166. Schokker E.P., Singh H., Pinder D.N., Creamer L.K. Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration. Journal of Agricultural and Food Chemistry 2000, 10:233-240.
167. Sharma A.K., Paramasivam M., Srinivasan A., Yadav M.P., Singh T.P. Three-dimensional structure of mare diferric lactoferrin at 2.6 Å resolution. Journal of Molecular Biology 1999, 289:303-317.
168. Shiraki K., Nishikawa K., Goto Y. Trifluoroethanol-induced stabilization of the α-helical structure of β-lactoglobulin: implication for non-hierarchical protein folding. Journal of Molecular Biology 1995, 245:180-194.
169. Shrake A., Frazier D., Schwarz F.P. Thermal stabilization of human albumin by medium- and short-chain n-alkyl fatty acid anions. Biopolymers 2006, 81:235-248.
170. Simard J.R., Zunszain P.A., Ha C.E., Yang J.S., Bhagavan N.V., Petitpas I., Curry S., Hamilton J.A. Locating high-affinity fatty acid-binding sites on albumin by X-ray crystallography and NMR spectroscopy. Proceedings of the National Academy of Sciences of the United States of America 2005, 102:17958-17963.
171. Skibsted L.H., Orlien V., Stapelfeldt H. Temperature effects on pressure denaturation of β-lactoglobulin. Milchwissenschaft 2007, 62:13-15.
172. Spector A.A. Fatty-acid binding to plasma albumin. Journal of Lipid Research 1975, 16:165-179.
173. Stapelfeldt H., Skibsted L.H. Pressure denaturation and aggregation of β-lactoglobulin studied by intrinsic fluorescence depolarization, Rayleigh scattering, radiationless energy transfer and hydrophobic fluoroprobing. Journal of Dairy Research 1999, 66:545-558.
174. Stapelfeldt H., Petersen P.H., Kristiansen K.R., Qvist K.B., Skibsted L.H. Effect of high hydrostatic pressure on the enzymic hydrolysis of β-lactoglobulin B by trypsin, thermolysin and pepsin. Journal of Dairy Research 1996, 63:111-118.
175. Steinrauf L.K. Structures of monoclinic lysozyme iodide at 1.6 Å and of triclinic lysozyme nitrate at 1.1 Å. Acta Crystallographica Section D: Biological Crystallography 1998, D54:767-779.
176. Strom M.B., Rekdal O., Svendsen J.S. Antibacterial activity of 15-residue lactoferricin derivatives. Journal of Peptide Research 2000, 56:265-274.
177. Strom M.B., Haug B.E., Rekdal O., Skar M.L., Stensen W., Svendsen J.S. Important structural features of 15-residue lactoferricin derivatives and methods for improvement of antimicrobial activity. Biochemistry and Cell Biology 2002, 80:65-74.
178. Sun C., Yang J., Wu X., Huang X., Wang F., Liu S. Unfolding and refolding of bovine serum albumin induced by cetylpyridinium bromide. Biophysical Journal 2005, 88:3518-3524.
179. Svensson M., Hakansson A., Mossberg A.K., Linse S., Svanborg C. Conversion of alpha-lactalbumin to a protein inducing apoptosis. Proceedings of the National Academy of Sciences of the United States of America 2000, 97:4221-4226.
180. Tanaka N., Kunugi S. Effect of pressure on the deuterium exchange reaction of α-lactalbumin and β-lactoglobulin. International Journal of Biological Macromolecules 1996, 18:33-39.
181. Tanaka N., Nishizawa H., Kunugi S. Structure of pressure-induced denatured state of human serum albumin: a comparison with the intermediate in urea-induced denaturation. Biochimica et Biophysica, Acta Protein Structure and Molecular Enzymology 1997, 1338:13-20.
182. Tanford C., Nozaki Y. Physico-chemical comparison of β-lactoglobulins A and B. Journal of Biological Chemistry 1959, 234:2874-2877.
183. Tanford C., Bunville L.G., Nozaki Y. Reversible transformation of β-lactoglobulin at pH 7.5. Journal of the American Chemical Society 1959, 81:4032-4036.
184. Tanford C., De P.K., Taggart V.G. The role of the α-helix in the structure of proteins. Optical rotatory dispersion of β-lactoglobulin. Journal of the American Chemical Society 1960, 82:6028-6034.
185. Tayyab S., Sharma N., Mushahid Khan M. Use of domain specific ligands to study urea-induced unfolding of bovine serum albumin. Biochemical and Biophysical Research Communications 2000, 277:83-88.
186. Thomas P.D., Dill K.A. Local and nonlocal interactions in globular proteins and mechanisms of alcohol denaturation. Protein Science 1993, 2:2050-2065.
187. Tromelin A., Guichard E. Interaction between flavor compounds and β-lactoglobulin: approach by NMR and 2D/3D-QSAR studies of ligands. Flavour and Fragrance Journal 2006, 21:13-24.
188. Tsuge H., Ago H., Noma M., Nitta K., Sugai S., Miyano M. Crystallographic studies of a calcium binding lysozyme from equine milk at 2.5 Å resolution. Journal of Biochemistry 1992, 111:141-143.
189. 15N chemical shifts for bovine β-lactoglobulin: secondary structure and topology of the native state is retained in a partially unfolded form. Journal of Biomolecular NMR 1998, 12:89-107.
190. Uhrínová S., Smith M.H., Jameson G.B., Uhrín D., Sawyer L., Barlow P.N. Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochemistry 2000, 39:3565-3574.
191. van Hooijdonk T., Steijns J. Incorporation of bioactive substances into products: technological challenges. Bulletin of the International Dairy Federation 2002, 375:65-69.
192. Vant S.C., Glen N.F., Kontopidis G., Sawyer L., Schaschke C.J. Volumetric changes to the molecular structure of β-lactoglobulin processed at high pressure. High Temperatures-High Pressures 2002, 34:705-712.
193. Watanabe S., Sato T. Effects of free fatty acids on the binding of bovine and human serum albumin with steroid hormones. Biochimica et Biophysica Acta-General Subjects 1996, 1289:385-396.
194. Wehbi Z., Perez M.-D., Sanchez L., Pocovi C., Barbana C., Calvo M. Effect of heat treatment on denaturation of bovine α-lactalbumin: determination of kinetic and thermodynamic parameters. Journal of Agricultural and Food Chemistry 2005, 53:9730-9736.
195. Wu S.Y., Perez M.D., Puyol P., Sawyer L. β-Lactoglobulin binds palmitate within its central cavity. Journal of Biological Chemistry 1999, 274:170-174.
196. Yalcin A.S. Emerging therapeutic potential of whey proteins and peptides. Current Pharmaceutical Design 2006, 12:1637-1643.
197. Yang J., Dunker A.K., Powers J.R., Clark S., Swanson B.G. β-Lactoglobulin molten globule induced by high pressure. Journal of Agricultural and Food Chemistry 2001, 49:3236-3243.
198. Ye M.-Q., Yi T.-Y., Li H.-P., Guo L.-L., Zou G.-L. Study on thermal and thermal chemical denaturation of bovine immunoglobulin G. Huaxue Xuebao 2005, 63:2047-2054.
199. Zhang H., Deligeersang, Guo J., Mu Z., Zhang Y., Zhu H. Denaturation of bovine milk IgG at high pressure and its stabilization. Shipin Kexue (Beijing) 1998, 19:10-12.
200. Zsila F. A new ligand for an old lipocalin: induced circular dichroism spectra reveal binding of bilirubin to bovine β-lactoglobulin. FEBS Letters 2003, 539:85-90.
201. Zsila F., Bikadi Z., Simonyi M. Retinoic acid binding properties of the lipocalin member β-lactoglobulin studied by circular dichroism, electronic absorption spectroscopy and molecular modeling methods. Biochemical Pharmacology 2002, 64:1651-1660.
202. Zsila F., Hazai E., Sawyer L. Binding of the pepper alkaloid piperine to bovine β-lactoglobulin: circular dichroism spectroscopy and molecular modeling study. Journal of Agricultural and Food Chemistry 2005, 53:10179-10185.