Abstract
In the past decade since the review in the 2nd edition of this book (Hambling et al., 1992), significant advances in our understanding of the structure and properties of β-lactoglobulin (β-Lg) have occurred, and it is the purpose of this review to revise and update that earlier chapter in the light of these later data. As space precludes mere addition of recent material, the interested reader is referred to the previous edition for a review of the work up to 1990. The aim, however, remains that of bringing together information from the last 65 years in order to discuss the possible biological function of this enigmatic milk protein.
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References
Adams, S.L., Barnett, D., Walsh, B.J., Pearce, R.J., Hill, D.J. and Howden, M.E.H. (1991) Human IgE-binding synthetic pep tides of bovine β-lactoglobulin and α-lactalbumin-in vitro cross-reactivity of the allergens. Immunol. Cell Biol., 69, 191–7.
Alexander, L.J. and Pace, C.N. (1971) A comparison of the denaturation of bovine β-lactoglobulins A and B and goat β-lactoglobulin. Biochem., 10, 2738–43.
Ali, S. and Clark, A.J. (1988) Characterization of the gene encoding ovine β-lactoglobulin. Similarity to the genes for retinol binding protein and other secretory proteins. J. Mol. Bioi., 199, 415–26.
Ananthanarayanan, V.S., Ahmad, F. and Bigelow, C.C. (1977) The denaturation of β-lactoglobulin-A at pH 2. Biochim. Biophys. Acta, 492, 194–203.
Anderson, L.J., Hayes, G., Pearse, M.J., Stewart, A.F., Willis, T.M. and McKinlay, A.G. (1989) Complete sequence of bovine β-lactoglobulin cDNA. Nucleic Acid Research, 17, 6739–45.
Antila, P., Paakkari, I., Mattila, M.J., Laukkanen, M., Pihlanto-Leppala, A., Mantsala, P. and Hellman, J. (1991) Opioid peptides derived from in vitro proteolysis of bovine whey proteins. Int. Dairy J., 1, 215–29.
Apenten, R.K.O. and Galani, D. (1999) Is the rate of sulfur-disulfide exchange between the native β-lactoglobulin and PDS related to protein conformational stability? Int. J. Food Sci. Technol., 34, 483–6.
Apenten, R.K.O. and Galani, D. (2000) Thermodynamic parameters for β-lactoglobulin dissociation over a broad temperature range at pH 2.6 and 7.0. Thermochim. Ada, 359, 181–8.
Arakawa, T. and Timasheff, S.N. (1987) Abnormal solubility behaviour of β-lactoglobulin: salting-in by glycine and NaCl. Biochem., 26, 5147–53.
Armstrong, J.M. and McKenzie, H.A. (1967) A method for modification of carboxyl groups in proteins: its application to the association of bovine β-lactoglobulin A. Biochim. Biophys. Ada, 147, 93–9.
Armstrong, J.M., McKenzie, H.A. and Sawyer, W.H. (1967) On the fractionation of β-lactoglobulin and α-lactalbumin. Biochim. Biophys. Acta, 147, 60–72.
Aschaffenburg, R. and Drewry, J. (1955) Occurrence of different β-lactoglobulins in cow’s milk. Nature, 176, 218–9.
Aschaffenburg, R. and Drewry, J. (1957) Improved method for the preparation of crystalline β-lactoglobulin and α-lactalbumin from cow’s milk. Biochem. J., 65, 273–7.
Aschaffenburg, R., Green, D.W. and Simmons, R.M. (1965) Crystal forms of β-lactoglobulin. J. Mol. Biol., 13, 194–201.
Ashworth, U.S., Ramaiah, G.D. and Keyes, M.C. (1996) Species difference in the composition of milk with special reference to the Northern fur seal. J. Dairy Sci., 49, 1206–11.
Askonas, B.A. (1954) Crystallization of goat β-lactoglobulin. Biochem. J., 58, 332–6.
Axelsson, I., Jakobsson, I., Lindberg, T. and Benediktsson, B. (1986) Bovine β-lactoglobulin in the human milk. Acta Paediatr. Scand., 75, 702–7.
Aymard, P., Durand, D. and Nicolai, T. (1996) The effect of temperature and ionicstrength on the dimerization of β-lactoglobulin. Int. J. Biol. Macromol., 19, 213–21.
Aymard, P., Nicolai, T., Durand, D. and Clark, A. (1999) Static and dynamic scattering of β-lactoglobulin aggregates formed after heat-induced denaturation at pH 2. Macromolecules, 32, 2542–52.
Azuma, N. and Yamauchi, K. (1991) Identification of a-lactalbumin and β-lactoglobulin in cynomolgus monkey (Macaca, fascicularis) milk. Comp. Biochem. Physiol. B, 99, 917–21.
Bain, J.A. and Deutsch, H.F. (1948) Studies on lactoglobulins. Arch. Biochem. Biophys., 16, 221–9.
Bairoch, A. and Apweiler, R. (2000) The SWISS-PROT protein sequence database and its supplement TREMBL in 2000. Nucleic Acids Res., 28, 45–8.
Baker, H.P. and Saroff, H.A. (1965) Binding of sodium ions to β-lactoglobulin. Biochem., 4, 1670–7.
Ball, G., Shelton, M.J., Walsh, B.J., Hill, D.J., Hosking, C.S. and Howden, M.E.H. (1994) A major continuous allergenic epitope of bovine β-lactoglobulin recognised by human IgE binding. Clin. Experimental Allergy, 24, 758–64.
Batt, C.A., Brady, J. and Sawyer, L. (1994) Design improvements of β-lactoglobulin. Trends Food Sci. Technol., 5, 261–5.
Baumy, J.J. and Brule, G. (1988) Binding of bivalent-cations to a-lactalbumin and β-lactoglobulin — effect of pH and ionic-strength. Lait, 68, 33–48.
Bawden, W.S., Passey, R.J. and Mackinlay, A.G. (1994) The genes encoding the major milk-specific proteins and their use in transgenic studies and protein engineering. In Biotechnology and Genetic Engineering Reviews — Vol. 12, (M.P. Tombs ed.) Intercept Ltd, UK, pp. 89–137.
Beg, O.U. (1995) Partial characterization of platypus (Ornithorhynchus anatinus) milk-proteins. Protein and Peptide Letters, 2, 431–4.
Bell, K. and McKenzie, H.A. (1964) β-Lactoglobulins. Nature, 204, 1275–9.
Bell, K. and McKenzie, H.A. (1967) The isolation and properties of bovine β-lactoglobulin C. Biochim. Biophys. Acta, 147, 109–22.
Bell, K., McKenzie, H.A., Muller, V., Rogers, C. and Shaw, D.C. (1981) Equine whey proteins. Comp. Biochem. Physiol., 68B, 225–36.
Bell, K., McKenzie, H.A., Murphy, W.H. and Shaw, D.C. (1970) β-Lactoglobulin Droughtmaster: a unique protein variant. Biochem. Biophys. Acta, 214, 427–36.
Bell, K., McKenzie, H.A. and Shaw, D.C. (1981a) Porcine β-lactoglobulin A and C. Mol. Cell. Biochem., 35, 103–11.
Bell, K., McKenzie, H.A. and Shaw, D.C. (1981b) Bovine β-lactoglobulin E, F and G of Bali (Banteng) cattle, Bos (Bibos) javanicus. Aust. J. Biol. Sci., 34, 133–47.
Belloque, J. and Smith, G.M. (1998) Thermal denaturation of β-lactoglobulin: a H-l NMR study. J. Agric. Food Chem., 46, 1805–13.
Bertino, E., Prandi, G.M., Fabris, C, Cavaletto, M., Dimartino, S., Cardaropoli, S., Calderone, V. and Conti, A. (1996) Human-milk proteins may interfere in ELISA measurements of bovine β-lactoglobulin in human-milk. Acta Paediatr., 85, 543–9.
Beste, G., Schmidt, F.S., Stibora, T. and Skerra, A. (1999) Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold. Proc. Natl. Acad. Sci. USA, 96, 1898–903.
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 perspective. In Milk Protein Polymorphism, (J.P. Hill and M. Boland eds.) Special Issue, 9702, International Dairy Federation, Brussels, pp. 100–9.
Blanch, E.W., Hecht, L. and Barron, L.D. (1999) New insight into the pH-dependent conformational changes in bovine β-lactoglobulin from Raman optical activity. Protein Sci., 8, 1362–7.
Blanchet, M.A., Bains, G., Pelosi, P., Pevsner, J., Snyder, S.H., Monaco, H.L. and Amzel, L.M. (1996) The 3-dimensional structure of bovine odorant bindingprotein and its mechanism of odor recognition. Nature Struct. Biol., 3, 934–9.
Bocskei, Z., Groom, C.R., Flower, D.R., Wright, C.E., Phillips, S.E.V., Cavaggioni, A., Findlay, J.B.C. and North, A.C.T. (1992) Pheromone binding to two rodent urinary proteins revealed by X-ray crystallography. Nature, 360, 186–8.
Bolognesi, M., Liberatori, J., Oberti, R. and Ungaretti, L. (1979) Preliminary crystallographic data on buffalo β-lactoglobulin. J. Mol. Biol., 131, 411–3.
Bos, M.A. and Nylander, T. (1996) Interaction between β-lactoglobulin and phospholipids at the air/water interface. Langmuir, 12, 2791–7.
Boudaud, N. and Dumont, J.P. (1996) Interaction between flavor components and β-lactoglobulin. ACS Symposium Series, 633, 90–7.
Braunitzer, G., Chen, R., Schrank, B. and Stangl, A. (1972) Die sequenzanalyse des β-lactoglobulins. Hoppe-Seyler’s Z. Physiol. Chem., 354, 867–8.
Braunitzer, G., Liberatori, J. and Kolde, H.-J. (1979) The primary structure of the β-lactoglobulin of the waterbuffalo (Bubalus arnee). Z. Naturforsch., 34c, 880–1.
Brew, K. and Campbell, P.N. (1967) The characterization of the whey proteins of guinea-pig milk, Biochem. J., 102, 258–64.
Brown, E.M. and Farrell, H.M., Jr. (1978) Interaction of β-lactoglobulin and cytochrome c: complex formation and iron reduction. Arch. Biochem. Biophys., 185, 156–64.
Brown, E.M., Carroll, R.J., Pfeffer, P.E. and Sampugna, J. (1983) Complex formation in sonicated mixtures of β-lactoglobulin and phosphatidylcholine. Lipids, 18, 111–8.
Brown, E.M., Pfeffer, P.E., Kumosinski, T.F. and Greenberg, R. (1988) Accessibility and mobility of lysine residues in β-lactoglobulin. Biochem., 27, 5601–10.
Brownlow, S., Cabrai, J.H.M., Cooper, R., Flower, D.R., Yewdall, S.J., Polikarpov, I., North, A.C.T. and Sawyer, L. (1997) Bovine β-lactoglobulin at 1.8 Å resolution — still an enigmatic lipocalin. Structure, 5, 481–95.
Bull, H.B. and Currie, B.T. (1946) Osmotic pressure of β-lactoglobulin solutions. J. Amer. Chem. Soc., 68, 742–7.
Burova, T.V., Choiset, Y., Tran, V. and Haertlé, T. (1998) Role of free Cysl21 in stabilization of bovine β-lactoglobulin B. Protein Eng., 11, 1065–73.
Burr, R., Moore, C.H. and Hill, J.P. (1996) Evidence of multiple glycosylation of bovine β-lactoglobulin by electrospray-ionization mass-spectrometry. Milchwissenschaft, 51, 488–92.
Busti, P., Gatti, C.A. and Delorenzi, N.J. (1998) Some aspects of β-lactoglobulin structural properties in solution studied by fluorescence quenching. Int. J. Biol. Macromol., 23, 143–8.
Byler, D.M. and Susi, H. (1986) Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers, 25, 469–87.
Caessens, P.W.J.R., Daamen, W.F., Gruppen, H., Visser, S. and Voragen, A.G.J. (1999) β-Lactoglobulin hydrolysis. 2. Peptide identification, SH/SS exchange, and functional properties of hydrolysate fractions formed by the action of plasmin. J. Agric. Food Chem., 47, 2980–90.
Casal, H.L., Kohler, U. and Mantsch, H.N. (1988) Structural and conformation changes of β-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta, 957, 11–20.
Cecil, R. and Ogston, A.G. (1949) The sedimentation constant, diffusion constant and molecular weight of lactoglobulin. Biochem. J., 44, 33–5.
Changani, S.D., Belmar-Beiny, M.T. and Fryer, P.J. (1997) Engineering and chemical factors associated with fouling and cleaning in milk processing. Exptl. Therm. Fluid Sci., 14, 392–406.
Chatel, J.M., Bernard, H., Clement, G., Frobert, Y., Batt, C.A., Gavalchin, J., Peltre, G. and Wal, J.M. (1996) Expression, purification and immunochemical characterization of recombinant bovine β-lactoglobulin, a major cow milk allergen. Mol. Immunol., 33, 1113–8.
Chaudhuri, B.N., Kleywegt, G.J., Bjorkman, J., Lehmanmckeeman, L.D., Oliver, J.D. and Jones, T.A. (1999) The structures of α(2u)-globulin and its complex with a hyaline droplet inducer. Acta Cryst., D55, 753–62.
Chiancone, E. and Gattoni, M. (1993) Selective removal of β-lactoglobulin directly from cows milk and preparation of hypoallergenic formulas — a bioaffinity method. Biotechnol. Appl. Biochem., 18, 1–8.
Cho, Y.J., Batt, C.A. and Sawyer, L. (1994a) Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem., 269, 11102–7.
Cho, Y.J., Gu, W., Watkins, S., Lee, S.P., Kim, T.R., Brady, J.W. and Batt, C.A. (1994b) Thermostable variants of bovine β-lactoglobulin. Protein Eng., 7, 263–70.
Chobert, J.M., Briand, L., Grinberg, V. and Haertlé, T. (1995) Impact of esterification on the folding and the susceptibility to peptic proteolysis of β-lactoglobulin. Biochim. Biophys. Acta, 1248, 170–6.
Christensen, L.K. (1952) Denaturation and enzymic hydrolysis of lactoglobulin. C. R. Lab. Carlsberg (Ser. Chim.), 28, 37–174.
Chu, L., MacLeod, A. and Ozimek, L. (1996) Effect of charcoal delipidization treatment of β-lactoglobulin on kinetics of β-lactoglobulin/retinoic acid complex and its tryptic hydrolysis. Milchwissenschaft, 51, 252–5.
Clark, A.J. (1996) Genetic-modification of milk-proteins. Amer. J. Clin. Nutr., 63, S633–S638.
Clark, A.J., Simons, P., Wilmut, I. and Lathe, R. (1987) Pharmaceuticals from transgenic livestock. Trends Biotechnol., 5, 20–4.
Clark, D.C., Wilde, P.J., Wilson, D.R. and Wustneck, R. (1992) The interaction of sucrose esters with β-lactoglobulin and β-casein from bovine-milk. Food Hydrocolloids, 6, 173–86.
Coke, M., Wilde, P.J., Russell, E.J. and Clark, D.C. (1990) The influence of surfacecomposition and molecular-diffusion on the stability of foams formed from protein surfactant mixtures. J. Coll. Interface Sci., 138, 489–504.
Collet, C. and Joseph, R. (1995) Exon organization and sequence of the genes encoding α-lactalbumin and β-lactoglobulin from the tammar wallaby (Macropodidae, Marsupialia). Biochem. Genet., 33, 61–72.
Conti, A., Godovac-Zimmermann, J., Liberatori, J. and Braunitzer, G. (1984) The primary structure of monomeric β-lactoglobulin I from horse colostrum (Equus caballus, Perissodactyla). Hoppe-Seyler’s Z. Physiol. Chem., 366, 1393–401.
Cornell, D.G. and Patterson, D.L. (1989) Interaction of phospholipids in monolayers with β-lactoglobulin adsorbed from solution. J. Agric. Food Chem., 37, 1455–9.
Cowan, S.W., Newcomer, M.E. and Jones, T.A. (1990) Crystallographic refinement of human serum retinol binding-protein at 2 A resolution. Prot. Struct. Funct. Genet., 8, 44–61.
Creamer, L.K. (1995) Effect of sodium dodecyl-sulfate and palmitic acid on the equilibrium unfolding of bovine β-lactoglobulin. Biochemistry, 34, 7170–6.
Creamer, L.K., Parry, D.A.D. and Malcolm, G.N. (1983) Secondary structure of bovine β-lactoglobulin B. Arch. Biochem. Biophys., 227, 98–105.
Creighton, T.E. (1980) Kinetic study of protein unfolding and refolding using urea gradient electrophoresis. J. Mol. Biol., 137, 61–80.
Crossett, B., Allen, W.R. and Stewart, F. (1996) A 19 kDa protein secreted by the endometrium of the mare is a novel member of the lipocalin family. Biochem. J., 320, 137–43.
Crowfoot, D.M. and Riley, D.P. (1938) An X-ray study of Palmer’s lactoglobulin. Nature, 141, 521–2.
Cunningham, L.W. and Nuenke, B.J. (1960) Analysis of modified β-lactoglobulins and ovalbumins prepared from the sulfenyl iodide intermediates. J. Biol. Chem., 235, 1711–5.
Cupo, J.F. and Pace, C.N. (1983) Conformational stability of mixed disulphide derivatives of β-lactoglobulin B. Biochem., 22, 2654–8.
D’Alfonso, L., Collini, M. and Baldini, G. (1999) Evidence of heterogeneous l-anilinonaphthalene-8-sulfonate binding to β-lactoglobulin from fluorescence spectroscopy. Biochim. Biophys. Acta, 1432, 194–202.
Dalgalarrondo, M., Dufour, E., Chobert, J.M., Bertrandharb, C. and Haertlé, T. (1995) Proteolysis of β-lactoglobulin and β-casein by pepsin in ethanolic media. Int. Dairy J., 5, 1–14.
Davies, D.T. (1974) The quantitative partition of the albumin fraction of milk serum proteins by gel chromotography. J. Dairy Res., 41, 217–28.
Davis, P.J. and Williams, S.C. (1998) Protein modification by thermal processing. Allergy, 53, 102–5.
de Wit and Klarenbeek, G. (1981) A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperatures up to 160°C. J. Dairy Res., 48, 293–302.
Deckmyn, H. and Preaux, G. (1978) Chain folding prediction of the bovine β-lactoglobulins. Arch. Int. Physiol. Biochim., 86, 938–9.
DeFutos, M., Molina, E. and Amigo, L. (1996) Applicability of capillary electrophoresis to the study of bovine β-lactoglobulin polymorphism. Milchwissenschaft, 51, 374–8.
Diaz de Villegas, M.C., Oria, R., Sala, F.J. and Calvo, M. (1987) Lipid binding by β-lactoglobulin of cow milk. Milchwissenschaft, 42, 357–8.
Dib, R., Chobert, J.M., Dalgalarrondo, M. and Haertlé, T. (1996) Secondary structure changes and peptic hydrolysis of β-lactoglobulin induced by diols. Biopolymers, 39, 23–30.
Dodin, G. Andrieux, M. and Alkabbani, H. (1990) Binding of ellipticine to β-lactoglobulin — a physicochemical study of the specific interaction of an antitumor drag with a transport protein. Eur. J. Biochem., 193, 697–700.
Dong, A., Matsuura, J., Allison, S.D., Chrisman, E., Manning, M.C. and Carpenter, J.F. (1996) Infrared and circular-dichroism spectroscopic characterization of structural differences between β-lactoglobulin-A and β-lactoglobulin-B. Biochem., 35, 1450–7.
Dufour, E., Bertrandharb, C. and Haertlé, T. (1993) Reversible effects of medium dielectric-constant on structural transformation of β-lactoglobulin and its retinol binding. Biopolymers, 33, 589–98.
Dufour, E., Genot, C. and Haertlé, T. (1994) β-Lactoglobulin binding-properties during its folding changes studied by fluorescence spectroscopy. Biochim. Biophys. Acta, 1205, 105–12.
Dufour, E. and Haertlé, T. (1990) Alcohol-induced changes of β-lactoglobulin retinol-binding stoichiometry. Protein Eng., 4, 185–90.
Dufour, E. and Haertlé, T. (1993) Temperature-induced folding changes of β-lactoglobulin in hydro-methanolic solutions. Int. J. Biol. Macromol., 15, 293–7.
Dufour, E., Marden, M.C. and Haertlé, T. (1990) β-Lactoglobulin binds retinol and protoporphyrin-IX at 2 different binding-sites. FEBS Lett., 277, 223–6.
Dufour, E., Roger, P. and Haertlé, T. (1992) Binding of benzo(α)pyrene, ellipticine and cis-parinaric acid to β-lactoglobulin — influence of protein modifications. J. Prot. Chem., 11, 645–52.
Dunnill, P. and Green, D.W. (1965) Sulphydryl groups and the N-R conformational change in β-lactoglobulin. J. Mol. Biol., 15, 147–51.
Dunnill, P., Green, D.W. and Simmons, R.M. (1966) Heavy-atom sulphydryl derivatives of oxy haemoglobin and β-lactoglobulin; factors affecting isomorphism of native and derivative crystals. J. Mol. Biol., 22, 135–44.
Dupont, M. (1965) Etude d’une etape reversible dans la thermo-denaturation de la β-lactoglobuline bovine A. Biochim. Biophys. Acta, 102, 500–13.
Elofsson, U.M., Dejmek, P. and Paulsson, M.A. (1996a) Heat-induced aggregation of beta-lactoglobulin studied by dynamic light-scattering. Int. Dairy J., 6, 343–57.
Elofsson, U.M., Paulsson, M.A., Sellers, P. and Arnebrant, T. (1996b) Adsorption during heat treatment related to the thermal unfolding aggregation of betalactoglobulins A and B. J. Coll. Interface Sci., 183, 408–15.
Evans, T.R.J. and Kaye, S.B. (1999) Retinoids: present role and future potential Brit. J. Cancer, 80, 1–8.
Farrell, H.M., Jr., Behe, M.J. and Enyaert, J.A. (1987) Binding of p-nitrophenyl phosphate and other aromatic compounds by β-lactoglobulin. J. Dairy Sci., 70, 252–8.
Farrell, H.M., Jr. and Thompson, M.P. (1990) β-Lactoglobulin and α-lactalbumin as potential modulators of mammary cellular-activity — a Ca2+-responsive model system using acid phosphoprotein phosphatases. Protoplasma, 159, 157–67.
Feligini, M., Parma, P., Aleandri, R., Greppi, G.F. and Enne, G. (1998) PCR-RFLP test for direct determination of β-lactoglobulin genotype in sheep. Animal Genetics, 29, 473–4.
Fernandez, F.M. and Oliver, G. (1988) Proteins present in llama milk. I. Quantitative aspects and general characteristics. Milchwissenschaft, 43, 299–302.
Fernandez-Espla, M.D., Lopez-Galvez, G. and Ramos, M. (1993) Isolation of ovine β-lactoglobulin genetic-variants by chromatofocusing — heterogeneity of β-lactoglobulin-A. Chromatographia, 37, 43–6.
Ferry, J.D. and Oncley, J.L. (1941) Studies on the dielectric properties of protein solutions. III. Lactoglobulin. J. Amer. Chem. Soc., 63, 272–8.
Flower, D.R. (1996) The lipocalin protein family — structure and function. Biochem. J., 318, 1–14.
Fogolari, F., Ragona, L., Zetta, L., Romagnoli, S., Dekruif, K.G. and Molinari, H. (1998) Monomeric bovine β-lactoglobulin adopts a β-barrel fold at pH 2. FEBS Lett., 436, 149–54.
Fogolari, F., Ragona, L., Licciardi, S., Romagnoli, S., Michelutti, R., Ugolini, R. and Molinari, H. (2000) Electrostatic properties of bovine β-lactoglobulin. Protein-Struct. Funct. Genet., 39, 317–30.
Folch, J.M., Coll, A., Hayes, H.C. and Sanchez, A. (1996) Characterization of a caprine β-lactoglobulin pseudogene, identification and chromosomal localization by in-situ hybridization in goat, sheep and cow. Gene, 177, 87–91.
Forge, V., Hoshino, M., Kuwata, K., Arai, M., Kuwajima, K., Batt, C.A. and Goto, Y. (2000) Is folding of β-lactoglobulin non-hierarchic? Intermediate with nativelike β-sheet and non-native β-helix. J. Mol. Bioi., 296, 1039–51.
Fox, P.F. (1995) Heat-induced Changes in Milk, Special Issue, 9501, International Dairy Federation, Brussels.
Frapin, D., Dufour, E. and Haertlé, T. (1993) Probing the fatty-acid-binding site of β-lactoglobulins. J. Prot. Chem., 12, 443–9.
Frushour, B.G. and Koenig, L.J. (1975) Roman studies of the crystalline, solution and alkaline-denatured states of β-lactoglobulin. Biopolymers, 14, 649–62.
Fugate, R.D. and Song, P.-S. (1980) Spectroscopic characterization of β-lactoglobulin-retinol complex. Biochim. Biophys. Acta, 625, 28–42.
Fujiwara, K., Arai, M., Shimizu, A., Ikeguchi, M., Kuwajima, K. and Sugai, S. (1999) Folding-unfolding equilibrium and kinetics of equine β-lactoglobulin: equivalence between the equilibrium molten globule state and a burst-phase folding intermediate. Biochemistry, 38, 4455–63.
Fukushima, Y., Kawata, Y., Onda, T. and Kitagawa, M. (1997) Consumption of cow milk and egg by lactating women and the presence of β-lactoglobulin and ovalbumin in breast milk. Amer. J. Clin. Nutr., 65, 30–5.
Futterman, S. and Heller, J. (1972) The enhancement of fluorescence and the decreased susceptibility to enzymic oxidation of bovine serum albumin, β-lactoglobulin and the retinol-binding protein of human plasma. J. Biol. Chem., 247, 5168–72.
Gallagher, D.P., Lynch, M.G. and Mulvihill, D.M. (1996) Porcine β-lactoglobulin does not undergo thermally-induced gelation. J. Dairy Res., 63, 479–82.
Ganfornina, M.D., Gutierrez, G., Bastiani, M. and Sanchez, D. (2000) A phylogenetic analysis of the lipocalin protein family. Mol. Biol. Evol., 17, 114–26.
Garde, J., Bell, S.C. and Eperon, I.C. (1991) Multiple forms of messenger-RNA encoding human pregnancy-associated endometrial α-2u-globulin, a β-lactoglobulin homolog. Proc. Natl. Acad. Sci. USA, 88, 2456–60.
Gaye, P., Hue-Delahaie, D., Mercier, J.-C, Soulier, S., Vilotte, J.L. and Furet, J.P. (1986) Ovine β-lactoglobulin messenger RNA: nucleotide sequence and mRNA levels during functional differentiation of the mammary gland. Biochimie, 68, 1097–107.
GayeSeye, M.D., Gadji, F., Dodin, G., Aaron, JJ. and Tine, A. (1997) Fluorescence studies of the binding of two natural alkaloids (cinchonine and cinchonidine) with β-lactoglobulin. J. Chim. Phys. Phys.-Chim. Biol., 94, 31–6.
Georges, C. and Guinand, S. (1960) Sur la dissociation reversible de la β2-lactoglobuline, a des pH superieurs a 5.5. 1. Etude par la diffusion de la lumiere. J. Chim. Phys., 57, 606–14.
Georges, C, Guinand, S. and Tonnelat, J. (1962) Etude thermodynamique de la dissociation reversible de la β-lactoglobuline B pour des pH superieurs a 5.5. Biochim. Biophys. Acta, 59, 737–9.
Gestin, M., Desbois, C, LeHuerouLuron, I., Rome, V., LeDrean, G., Lengagne, T., Roger, L., Mendy, F. and Guilloteau, P. (1997) In vitro hydrolysis by pancreatic elastases i and ii reduces β-lactoglobulin antigenicity. Lait, 77, 399–409.
Gezimati, J., Creamer, L.K. and Singh, H. (1997) Heat interactions and gelation of mixtures of β-lactoglobulin and α-lactalbumin. J. Agric. Food Chem., 45, 1130–6.
Ghose, A.C., Chaudhuri, S. and Sen, A. (1968) Hydrogen ion equilibria and sedimentation behaviour of goat β-lactoglobulins. Arch. Biochem. Biophys., 126, 232–43.
Gimel, J.C., Durand, D. and Nicolai, T. (1994) Structure and distribution of aggregates formed after heat-induced denaturation of globular-proteins. Macromolecules, 27, 583–9.
Godovac-Zimmermann, J. (1988) The strucural motif of β-lactoglobulin and retinol binding protein: a basic framework for binding and transport of small hydrophobic molecules? Trends Biochem. Sci., 13, 64–6.
Godovac-Zimmermann, J., Conti, A., James, L. and Napolitano, L. (1988) Microanalysis of the amino-acid sequence of monomeric β-lactoglobulin I from donkey (Equus asinus) milk. Biol. Chem. Hoppe-Seyler, 369, 171–9.
Godovac-Zimmermann, J., Conti, A., Liberatori, J. and Braunitzer, G. (1985a) Homology between the primary structures of β-lactoglobulins and human retinol binding protein: evidence for a similar biological function? Biol. Chem. Hoppe-Seyler, 366, 431–4.
Godovac-Zimmermann, J., Conti, A., Liberatori, J. and Braunitzer, G. (1985b) The amino acid sequence of β-lactoglobulin II from horse colostrum (Equus caballus, Perissodactyla): β-lactoglobulins are retinol-binding proteins. Biol. Chem. Hoppe-Seyler, 366, 601–8.
Godovac-Zimmermann, J., Conti, A. and Napolitano, L. (1987) The complete amino acid sequence of dimeric β-lactoglobulin from mouflon (Ovis ammon musimon) milk. Biol. Chem. Hoppe-Seyler, 368, 1313–9.
Godovac-Zimmermann, J., Krause, I., Buchberger, J., Weiss, G. and Kloster-meyer, H. (1990) Genetic-variants of bovine β-lactoglobulin — a novel wild-type β-lactoglobulin W and its primary sequence. Biol. Chem. Hoppe-Seyler, 371, 255–60.
Godovac-Zimmermann, J., Krause, I., Baranyi, M., FischerFruhholz, S., Juszczak, J., Erhardt, G., Buchberger, J. and Klostermeyer, H. (1996) Isolation and rapid sequence characterization of two novel bovine β-lactoglobulins I and J. J. Prot. Chem., 15, 743–50.
Goetz, D.H., Willie, S.T., Armen, R.S., Bratt, T., Borregaard, N. and Strong, R.K. (2000) Ligand preference inferred from the structure of neutrophil gelatinase associated lipocalin. Biochem., 39, 1935–41.
Gorbunoff, M.J. (1967) Exposure of tyrosine residues in proteins. Reaction of cyanuric fluoride with ribonuclease, α-lactalbumin and β-lactoglobulin. Biochem., 6, 1606–15.
Green, D.W. and Aschaffenburg, R. (1959) Twofold symmetry of the β-lactoglobulin molecule in crystals. J. Mol. Biol., 1, 54–64.
Green, D.W., Aschaffenburg, R., Camerman, A., Coppola, J.C., Diamand, R.D., Dunnill, P., Simmons, R.M., Komorowski, E.S., Sawyer, L., Turner, E.M.C. and Woods, K.F. (1979) Structure of bovine β-lactoglobulin at 6Å resolution. J. Mol. Biol., 131, 375–97.
Green, D.W., North, A.C.T. and Aschaffenburg, R. (1956) Crystallography of β-lactoglobulin from cows’ milk. Biochim., Biophys. Acta, 21, 583–5.
Greenberg, R. and Kalan, E.B. (1965) Studies on β-lactoglobulins A, B and C. II. Preparation of modified proteins by treatment with carboxypeptidase A. Biochem., 4, 1660–6.
Greene, R.F. and Pace, C.N. (1974) Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, α-chymotrypsin and β-lactoglobulin. J. Biol. Chem., 249, 5388–93.
Griffin, W.G., Griffin, M.C.A., Martin, S.R. and Price, J. (1993) Molecular basis of thermal aggregation of bovine β-lactoglobulin-A. J. Chem. Soc. Farad. Trans., 89, 3395–406.
Griko, Y.V. and Kutyshenko, V.P. (1994) Differences in the processes of β-lactoglobulin cold and heat denaturations. Biophys. J., 67, 356–63.
Grosclaude, F., Mahe, M.-F., Mercier, J.-C, Bonnemarie, J. and Teissier, J.H. (1976) Polymorphisme des lactoproteines de bovines nepalais. Ann. Genet. Sel. Anim., 8, 461–79.
Groves, M.L., Hipp, N.J. and McMeekin, T.L. (1951) Effect of pH on the denaturation of β-lactoglobulin and its dodecyl sulphate derivative. J. Amer. Chem. Soc., 73, 2790–3.
Guo, M.R., Fox, P.F., Flynn, A. and Kindstedt, P.S. (1995) Susceptibility of β-lactoglobulin and sodium caseinate to proteolysis by pepsin and trypsin. J. Dairy Sci., 78, 2336–44.
Hallberg, R.K. and Dubin, P.L. (1998) Effect of pH on the binding of β-lactoglobulin to sodium polystyrenesulfonate. J. Phys. Chem., B, 102, 8629–33.
Halliday, J.A., Bell, K. and Shaw, D.C. (1991) The complete amino-acid-sequence of feline β-lactoglobulin-II and a partial revision of the equine β-lactoglobulin-II sequence. Biochim. Biophys. Acta, 1077, 25–30.
Halpin, M.I. and Richardson, T. (1985) Selected functionality changes of β-lactoglobulin upon esterification of side chain carboxyl groups. J. Dairy. Sci., 68, 3189–98.
Hamada, D. and Goto, Y. (1997) The equilibrium intermediate of β-lactoglobulin with non-native a-helical structure. J. Mol. Biol., 269, 479–87.
Hamada, D., Kuroda, Y., Tanaka, T. and Goto, Y. (1995) High helical propensity of the peptide-fragments derived from β-lactoglobulin, a predominantly β-sheet protein. J. Mol. Biol., 254, 737–46.
Hamada, D., Segawa, S. and Goto, Y. (1996) Normative a-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nature Struct. Biol., 3, 868–73.
Hambling, S.G., McAlpine, A.S. and Sawyer, L. (1992) β-Lactoglobulin. In: Advanced Dairy Chemistry I. Proteins, 2nd edn, (P.F. Fox ed.) Elsevier Applied Science, London, pp. 140–91.
Hattori, M., Aiba, Y., Nagasawa, K. and Takahashi, K. (1996) Functional improvement of alginic acid by conjugating with β-lactoglobulin. J. Food Sci., 61, 1171–6.
Hattori, M., Ametani, A., Katakura, Y., Shimizu, M. and Kaminogawa, S. (1993) Unfolding/refolding studies on bovine β-lactoglobulin with monoclonal antibodies as probes — does a renatured protein completely refold. J. Biol. Chem., 268, 22414–9.
Hattori, M., Nagasawa, K., Ametani, A., Kaminogawa, S. and Takahashi, K. (1994) Functional-changes in β-lactoglobulin by conjugation with carboxymethyl dextran. J. Agric. Food Chem., 42, 2120–5.
Hayakawa, I., Linko, Y.Y. and Linko, P. (1996) Mechanism of high-pressure denaturation of proteins. Lebens.-Wissen. Technol., 29, 756–62.
Heddleson, R.A., Alien, J.C., Wang, Q.W. and Swaisgood, H.E. (1997) Purity and yield of β-lactoglobulin isolated by an n-retinyl-celite bioaffinity column. J. Agric. Food Chem., 45, 2369–73.
Hemley, R., Kohler, B.E. and Siviski, P. (1979) Absorption spectra for the complexes formed from vitamin-A and β-lactoglobulin. Biophys. J., 28, 447–55.
Hennighausen, L.G. and Sippel, A.E. (1982) Mouse whey acidic protein is a novel member of the family of ‘four-disulphide core’ proteins. Nucl. Acid Res., 10, 2677–84.
Herskovits, T.T., Townend, R. and Timasheff, S.N. (1964) Molecular interactions in β-lactoglobulin. IX. Optical rotatory dispersion of the genetic variants in different states of association.J. Amer. Chem. Soc., 86, 4445–52.
Hill, A.R. (1989) The β-lactoglobulin-K-casein complex. Can. Inst. Food Sci. Technol. J., 11, 120–3.
Hill, J.P., Boland, M.J., Creamer, L.K., Anema, S.G., Otter, D.E., Paterson, G.R., Lowe, R., Motion, R.L. and Thresher, W.C. (1996) Effect of the bovine β-lactoglobulin phenotype on the properties of β-lactoglobulin, milk composition and dairy products. In Macromolecular Interactions in Food Technology, (N. Parris, A. Kato, L.K. Creamer and J. Pearce eds.) ACS Symposium Series, 650, 281–94.
Hill, R.M. and Briggs, D.R. (1956) A study of the interaction of n-octylbenzene-p-sulphonate with β-lactoglobulin. J. Amer. Chem. Soc., 78, 1590–7.
Hilquist, A.J., Dan, M.O. and Kresheck, G.C. (1982) Influence of surfactants on the conformation of β-lactoglobulin B using circular dichroism. Biopolymers, 21, 895–908.
Hui Bon Hoa, G., Douzou, P. and Pantaloni, C. (1973) Transformations alcalines de la β-lactoglobulies en milieau hydro-alcoolique a basses temperatures. Biochemie, 55, 269–76.
Hodgkin, D.C. and Riley, D.P. (1968) Some ancient history of protein X-ray analysis. In Structural Chemistry and Molecular Biology, (A. Rich and N. Davidson eds.) Freeman, New York. pp. 15–28.
Holt, C, McPhail, D., Nylander, T., Otte, J., Ipsen, R.H., Bauer, R., Ogendal, L., Olieman, K., Dekruif, C.G., Leonil, J., Molle, D., Henry, G., Maubois, J.L., Perez, M.D., Puyol, P., Calvo, M., Bury, S.M., Kontopidis, G., McNae, I., Sawyer, L., Ragona, L., Zetta, L., Molinari, H., Klarenbeek, B., Jonkman, M.J., Moulin, J. and Chatterton, D. (1999) Some physico-chemical properties of nine commercial or semi-commercial whey protein concentrates, isolates and fractions. Int. J. Food Sci. Technol., 34, 587–601.
Holt, C, Waninge, R., Sellers, P., Paulsson, M., Bauer, R., Ogendal, L., Roefs, S.P.F.M., van Mill, P., de Kruif, C.G., Leonil, J., Fauquant, J. and Maubois, J.L. (1998) Comparison of the effect of heating on the thermal denaturation of nine different β-lactoglobulin preparations of genetic variants A, B or A/B, as measured by microcalorimetry. Int. Dairy J., 8, 99–104.
Horisberger, M. and Vauthey, M. (1984) Labelling of colloidal gold with protein: A quantitative study using β-lactoglobulin. Histochemistry, 22, 123–8.
Huang, Q., Coleman, J.W. and Stanworth, D.R. (1985) Investigation of the allergenicity of β-lactoglobulin and its cleavage fragments. Int. Arch. All. Appl. Immun., 78, 337–45.
Huber, R., Schneider, M., Mayer, I., Muller, R., Deutzmann, R., Suter, F., Zuber, H., Falk, H. and Kayser, H. (1987) Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 Å. J. Mol. Biol., 198, 499–513.
Hummer, G., Garde, S., Garcia, A.E., Paulaitis, M.E. and Pratt, L.R. (1998) The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl. Acad. Sci., USA, 95, 1552–5.
Hunziker, H.G. and Tarassuk, N.P. (1965) Chromatographie evidence for heat induced interaction of α-lactalbumin and β-lactoglobulin. J. Dairy Sci., 48, 733–44.
Hyttinen, J.M., Korhonen, V.P., Hiltunen, M.O., Myohanen, S. and Janne, J. (1998) High-level expression of bovine β-lactoglobulin gene in transgenic mice. J. Biotechnol., 61, 191–8.
Iametti, S., Degregori, B., Vecchio, G. and Bonomi, F. (1996) Modifications occur at different structural levels during the heat denaturation of β-lactoglobulin. Eur. J. Biochem., 237, 106–12.
Iametti, S., Scaglioni, L., Mazzini, S., Vecchio, G. and Bonomi, F. (1998) Structural features and reversible association of different quaternary structures of β-lactoglobulin. J. Agric. Food Chem., 46, 2159–66.
Iametti, S., Transidico, P., Bonomi, F., Vecchio, G., Pittia, P., Rovere, P. and DallAglio, G. (1997) Molecular modifications of β-lactoglobulin upon exposure to high pressure. J. Agric. Food Chem., 45, 23–9.
Ibanez, E., Folch, J.M., Vidal, F., Coll, A., Santalo, J., Egozcue, J. and Sanchez, A. (1997) Expression of caprine β-lactoglobulin in the milk of transgenic mice. Transgenic Res., 6, 69–74.
Ikeguchi, M., Kato, S., Shimizu, A. and Sugai, S. (1997) Molten globule state of equine β-lactoglobulin. Proteins — Struct. Funct. and Genet., 27, 567–75.
Ivanov, V.N., Judinkova, E.S. and Gorodetsky, S.I. (1988) Molecular cloning of bovine β-lactoglobulin cDNA. Biol. Chem. Hoppe-Seyler, 369, 425–9.
Jadot, M., Laloux, J., Burny, A. and Kettmann, R. (1992) Detection of bovine β-lactoglobulin genomic variants by the polymerase chain-reaction method and molecular hybridization. Animal Genet., 23, 77–9.
Jakob, E. and Puhan, Z. (1992) Technological properties of milk as influenced by genetic polymorphism of milk proteins — a review. Int. Dairy J., 2, 157–78.
Jamieson, A.C., Vandeyar, M.A., Kang, Y.C., Kinsella, J.E. and Batt, C.A. (1987) Cloning and nucleotide-sequence of the bovine β-lactoglobulin gene. Gene, 61, 85–90.
Jang, H.D. and Swaisgood, H.E. (1990) Analysis of ligand-binding and β-lactoglobulin denaturation by chromatography on immobilized trans-retinal. J. Dairy Sci., 73, 2067–74.
Jenness, R. (1979) Comparative aspects of milk proteins. J. Dairy Res., 46, 197–210.
Jenness, R. (1985) Biochemical and nutritional aspects of milk and colostrum. In Lactation, (B.L. Larson ed.) The Iowa State University Press, Ames, pp. 164–97.
Jenness, R., Phillips, N.I. and Kalan, E.B. (1967) Immunochemical comparison of β-lactoglobulins. Fed. Proc., 26, 340.
Jeyarajah, S. and Allen, J.C. (1994) Calcium binding and salt-induced structural changes of native and preheated β-lactoglobulin. J. Agric. Food Chem., 42, 80–5.
Jones, M.N. and Wilkinson, A. (1976) The interaction between β-lactoglobulin and sodium n-dodecyl sulphate. Biochem. J., 153, 713–8.
Joss, L.A. and Ralston, G.B. (1996) β-Lactoglobulin-B — a proposed standard for the study of reversible self-association reactions in the analytical ultracentrifuge. Anal. Biochem., 236, 20–6.
Kalan, E.B. and Basch, J.J. (1969) Preparation of goat β-Lactoglobulin. J. Dairy Sci., 49, 406–9.
Kalan, E.B., Greenberg, R. and Walter, M. (1965) β-Lactoglobulins A, B and C. L. Comparison of chemical properties. Biochem., 4, 991–7.
Kalan, E.B., Kraeling, R.R. and Gerrits, R.J. (1971) Isolation and partial characterization of a polymorphic swine whey protein. Int. J. Biochem., 2, 232–44.
Kamata, N., Enomoto, A., Ishida, S., Nakamura, K., Kurisaki, J.I. and Kaminogawa, S. (1996) Comparison of pH and ionic-strength dependence of interactions between monoclonal-antibodies and bovine β-lactoglobulin. Biosci. Biotechnol. and Biochem., 60, 25–9.
Kaminogawa, S. (1996) Food allergy, oral tolerance and immunomodulation — their molecular and cellular mechanisms. Biosci. Biotechnol. Biochem., 60, 1749–56.
Kaminogawa, S., Shimizu, M., Ametani, A., Hattori, M., Ho, O., Hachimura, S., Nakamura, Y., Totsuka, M. and Yamauchi, K. (1989) Monoclonal-antibodies as probes for monitoring the denaturation process of bovine β-lactoglobulin. Biochim. Biophys. Acta, 998, 50–6.
Karlsson, C.A.C., Wahlgren, M.C. and Tragardh, A.C. (1996) β-Lactoglobulin fouling and its removal upon rinsing and by SDS as influenced by surface characteristics, temperature and adsorption time. J. Food Eng., 30, 43–60.
Katakura, Y., Ametani, A., Totsuka, M., Nagafuchi, S. and Kaminogawa, S. (1999) Accelerated secretion of mutant β-lactoglobulin in Saccharomyces cerevisiae resulting from a single ammo acid substitution. Biochim. Biophys. Acta, 1432, 302–12.
Katakura, Y., Totsuka, M., Ametani, A. and Kaminogawa, S. (1994) Tryptophan-19 of β-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure. Biochim. Biophys. Acta, 1207, 58–67.
Katakura, Y., Totsuka, M., Ametani, A. and Kaminogawa, S. (1997) A small variance in the antigenicity but not function of recombinant β-lactoglobulin purified from the culture supernatant of transformed yeast cells. Cytotechnology, 23, 133–41.
Kessler, E. and Brew, K. (1970) The whey proteins of pig’s milk isolation and characterization of a β-lactoglobulin. Biochim. Biophys. Acta, 200, 449–58.
Kiddy, C.A., Rollins, R.E. and Zikakis, J.P. (1972) Discontinuous polyacrylamide electrophoresis for β-lactoglobulin of cow milk. J. Dairy Sci., 55, 1506–7.
Kim, J.C. and Lund, D.B. (1998) Milk protein stainless steel interaction relevant to the initial stage of fouling in thermal processing. J. Food Process Eng., 21, 369–86.
Kim, S.C., Olson, N.F. and Richardson, T. (1990) Thiolation of β-lactoglobulin with N-acetylhomocysteine thiolactone (n-AHTL) and S-acetylmercaptosuccinic anhydride. Milchwissenschaft, 45, 580–3.
Kim, T.R., Goto, Y., Hirota, N., Kuwata, K., Denton, H., Wu, S.Y., Sawyer, L. and Batt, C.A. (1997) High-level expression of bovine β-lactoglobulin in Pichia pastoris and characterisation of its physical properties. Protein Eng., 10, 1339–45.
Kinsella, J.E. and Whitehead, D.M. (1989) Proteins in whey: chemical, physical and functional properties. Adv. Food Nutr. Res., 33, 343–438.
Kobayashi, T., Ikeguchi, M. and Sugai, S. (2000) Molten globule structure of equine β-lactoglobulin by hydrogen exchange. J. Mol. Biol., 299, 757–70.
Kontopidis, G., Holt, C. and Sawyer, L. (2002) The ligand-binding site of bovine β-lactoglobulin: Evidence for a function? J. Mol., Biol., 318, 1043–55.
Korhonen, V.P., Tolvanen, M., Hyttinen, J.M., UusiOukari, M., Sinervirta, R., Alhonen, L., Jauhiainen, M., Janne, O.A. and Janne, J. (1997) Expression of bovine β-lactoglobulin human erythropoietin fusion protein in the milk of transgenic mice and rabbits. Eur. J. Biochem., 245, 482–9.
Koritz, T.N., Suzuki, S. and Coomb, R.R.A. (1987) Antigenic stimulation with proteins of cows’ milk via the oral route in guinea-pigs and rats. 1. Measurement of antigenically intact β-lactoglobulin and casein in the gastrointestinal contents of duodenum, jejunum and ileum. Int. Arch. Allergy Appl. Immunol., 82, 72–5.
Kraulis, P.J. (1991) MOLSCRIPT — a program to produce both detailed and schematic plots of protein structures. J. Appl. Cryst., 24, 946–50.
Kristensen, A., Nylander, T., Paulsson, M. and Carlsson, A. (1997) Calorimetric studies of interactions between β-lactoglobulin and phospholipids in solutions. Int. Dairy J., 7, 87–92.
Kristiansen, K.R., Otte, J., Ipsen, R. and Qvist, K.B. (1998) Large-scale preparation of β-lactoglobulin A and B by ultrafiltration and ion-exchange chromatography. Int. Dairy J., 8, 113–8.
Kunz, C. and Lönnerdal, B. (1994) Isolation and characterization of a 21 kDa wheyprotein in rhesus-monkey (Macaca mulatta) milk. Comp. Biochem. Physiol. B, 108, 463–9.
Kurisaki, J., Nakamura, S., Kaminogawa, S. and Yamauchi, K. (1982) The antigenic properties of β-lactoglobulin examined with mouse IgE antibody. Agric. Biol. Chem., 46, 2069–75.
Kurisaki, J., Nakamura, S., Kaminogawa, S., Yamauchi, K., Watanabe, S., Hotta, K. and Hattori, M. (1985) Antigenicity of modified β-lactoglobulin examined by three different assays. Agric. Biol. Chem., 49, 1733–7.
Kuwajima, K., Yamaya, H., Miwa, S., Sugai, S. and Nagamura, T. (1987) Rapid formation of secondary structure framework in protein folding studied by stopped-flow circular-dichroism. FEBS Lett., 221, 115–8.
Kuwata, K., Hoshino, M., Era, S., Batt, C.A. and Goto, Y. (1998) α → β transition of β-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol., 283, 731–9.
Kuwata, K., Hoshino, M., Forge, V., Era, S., Batt, C.A. and Goto, Y. (1999) Solution structure and dynamics of bovine β-lactoglobulin A. Protein Sci., 8, 2541–5.
Kuzmanoff, K.M. and Beattie, C.W. (1991) Isolation of monoclonal-antibodies monospecific for bovine β-lactoglobulin. J. Dairy Sci., 74, 3731–40.
Laligant, A., Marti, J., Cheftel, J.C., Dumay, E. and Cuq, J.L. (1995) Detection of conformational modifications of heated β-lactoglobulin by immunochemical methods. J. Agric. Food Chem., 43, 2896–903.
Lamiot, E., Dufour, E. and Haertlé, T. (1994) Insect sex-pheromone binding by bovine β-lactoglobulin. J. Agric. Food Chem., 42, 695–9.
Lange, D.C., Kothari, R., Patel, R.C. and Patel, S.C. (1998) Retinol and retinoic acid bind to a surface cleft in bovine β-lactoglobulin: a method of binding site determination using fluorescence resonance energy transfer. Biophys. Chem., 74, 45–51.
Larson, B.L. and Jenness, R. (1952) Characterization of the sulphydryl groups and the kinetics of the heat denaturation of crystalline β-lactoglobulin. J. Amer. Chem. Soc., 74, 3090–3.
Law, A.J.R. (1995) Heat denaturation of bovine, caprine and ovine whey proteins. Milchwissenschaft, 50, 384–8.
Lebenthal, E., Laor, J., Lewitus, Z., Matoth, Y. and Freier, S. (1970) Gastrointestinal protein loss in allergy to cows’ milk β-lactoglobulin. Isr. J. Med. Sci., 6, 506–10.
Lee, S.P., Cho, Y.J. and Batt, C.A. (1993) Enhancing the gelation of β-lactoglobulin. J. Agric. Food Chem., 41, 1343–8.
Lee, S.P., Kim, D.S., Watkins, S. and Batt, C.A. (1994) Reducing whey syneresis in yogurt by the addition of a thermolabile variant of β-lactoglobulin. Biosci. Biotechnol. Biochem., 58, 309–13.
Leonil, J., Molle, D., Fauquant, J., Maubois, J.L., Pearce, R.J. and Bouhallab, S. (1997) Characterization by ionization mass spectrometry of lactosyl β-lactoglobulin conjugates formed during heat treatment of milk and whey and identification of one lactose-binding site. J. Dairy Sci., 80, 2270–81.
Li, C.H. (1946) Electrophoretic inhomogeneity of crystalline β-lactoglobulin. J. Amer. Chem. Soc., 68, 2746–7.
Li, H., Hardin, C.C. and Foegeding, E.A. (1994) NMR-studies of thermaldenaturation and cation-mediated aggregation of β-lactoglobulin. J. Agric. Food Chem., 42, 2411–20.
Liberatori, J., Guidetti, L.M. and Conti, A. (1979) Immunochemical studies on β-lactoglobulins. Precipitin reactions of sow’s and mare’s mammary secretions against anti-bovine β-lactoglobulin antiserum. Boll. Soc. It. Biol. Sper., 55, 815–21.
Liberatori, J., Morisio, L., Guetti, I.D., Conti, A. and Napolitano, L. (1979) β-Lactoglobulins in the mammary secretions of camel (Camelus dromedarius) and she-ass. Immunological detection and preliminary physico-chemical characterization. Boll. Soc. It. Biol. Sper., 55, 1369–73.
Lien, S., Alestrom, P., Steine, T., Langsrud, T., Vegarud, G. and Rogne, S. (1990) A method for β-lactoglobulin genotyping of cattle. Livestock Prod. Sci., 25, 173–6.
Lontie, R. and Préaux, G. (1966) Polarimetric investigation of β-lactoglobulin A and B and of the reactivity of their thiol groups. Protides Biol. Fluids, 14, 475–82.
Lovrien, R. and Anderson, W.F. (1969) Resolution of binding sites in β-lactoglobulin. Arch. Biochem. Biophys., 131, 139–44.
Lowe, R., Anema, S.G., Paterson, G.R. and Hill, J.P. (1995) Simultaneous separation of the β-lactoglobulin-A, β-lactoglobulin-B and β-lactoglobulin-C variants using polyacrylamide-gel electrophoresis. Milchwissenschaft, 50, 663–6.
Lyster, R.L.J. (1972) Reviews of the progress of dairy science. Section C. Chemistry of milk proteins. J. Dairy Res., 39, 279–318.
Lyster, R.L.J. and Wheelock, J.V. (1967) Occurrence of milk proteins in urine of cows during an extended milking interval. J. Dairy Res., 34, 27–30.
MacLeod, A., Fedio, W.M., Chu, L. and Ozimek, L. (1996) Binding of retinoic acid to β-lactoglobulin variant-A and variant-B — effect of peptic and tryptic digestion on the protein ligand complex. Milchwissenschaft, 51, 3–7.
Mailliart, P. and Ribadeau-Dumas, B. (1988) Preparation of β-lactoglobulin and β-lactoglobulin-free proteins from whey retentate by NaCl salting out at low pH. J. Food Sci., 53, 743–5,52.
Mainferme, F., Préaux, G. and Lontie, R. (1971) Location of the disulphide bridges in the sequence of β-lactoglobulin A with CNBr and thermolysin. Arch. Int. Physiol. Biochim., 79, 840–1.
Manderson, G.A., Hardman, M.J. and Creamer, L.K. (1998) Effect of heat treatment on the conformation and aggregation of β-lactoglobulin A, B and C. J. Agric. Food Chem., 46, 5052–61.
Manderson, G.A., Hardman, M.J. and Creamer, L.K. (1999a) Effect of heat treatment on bovine β-lactoglobulin A, B and C explored using thiol availability and fluorescence. J. Agric. Food Chem., 47, 3617–27.
Manderson, G.A., Creamer, L.K. and Hardman, M.J. (1999b) Effect of heat treatment on the circular dichroism spectra of bovine β-lactoglobulin A, B and C. J. Agric. Food Chem., 47, 4557–67.
Marden, M.C., Dufour, E., Christova, P., Huang, Y., Leclerc-Lhostis, E. and Haertlé, T. (1994) Binding of heme-CO to bovine and porcine β-lactoglobulins. Arch. Biochem. Biophys., 311, 258–62.
Martial, J., Preaux, G. and Lontie, R. (1971) Location of the thiol group and of the disulphide bridges in the sequence of β-lactoglobulin B. Arch. Int. Physiol. Biochim., 79, 842–3.
Mata, L., Sanchez, L. and Calvo, M. (1996) Cadmium uptake by Caco-2 cells, effect of some milk components. Chemico-Biolog. Interact., 100, 277–88.
Mata, L., Sanchez, L. and Calvo, M. (1997) Interaction of mercury with human and bovine milk. Biosci. Biotechnol. Biochem., 61, 1641–5.
Mattarella, N.L. and Richardson, T.L. (1983) Physicochemical and functional properties of positively charged derivatives of bovine β-lactoglobulin. J. Agric. Food Chem., 31, 972–8.
Maubois, J.L., Leonil, J., Bouhallab, S., Molle, D. and Pearce, J.R. (1995) Characterisation by ionisation mass spectrometry of a lactosyl-β-lactoglobulin conjugate occurring during milk heating of whey. J. Dairy Sci., 78(Suppl.1), 133.
Maubois, J.L., Pion, R. and Ribadeau-Dumas, B. (1965) Preparation et etude de la β-lactoglobulin de brebis crystallisee B. Biochim. Biophys. Acta, 107, 501–10.
McAipine, A.S. and Sawyer, L. (1990) β-Lactoglobulin: a protein drug carrier? Biochem. Soc. Trans., 18, 879.
McClenaghan, M., Hitchin, E., Stevenson, E.M., Clark, A.J., Holt, C. and Leaver, J. (1999) Insertion of a casein kinase recognition sequence induces phosphorylation of ovine β-lactoglobulin in transgenic mice. Protein Eng., 12, 259–64.
McDougall, E.I. and Stewart, J.C. (1977) The state of aggregation of red deer (Cervus elaphus L.) β-lactoglobulin preparations near neutral pH. Biochem. J., 167, 45–51.
McKenzie, H.A. (1967) Milk proteins. Adv. Prot. Chem., 22, 234.
McKenzie, H.A. (1971) β-Lactoglobulins. In Milk Proteins: Chemistry and Molecular Biology, Volume II. (H.A. McKenzie ed.) Academic Press, New York, pp. 257–330.
McKenzie, H.A., Muller, V.J. and Treacy, G.B. (1983) “Whey” proteins of milk of the red (Macropus rufus) and Eastern grey (Macropus giganteus) kangaroo. Comp. Biochem. Physiol., 748, 259–71.
McKenzie, H.A. and Ralston, G.B. (1971) The denaturation of proteins: two states? reversible or irreversible?. Experientia, 27, 617–24.
McKenzie, H.A. and Ralston, G.B. (1973) Nature of products formed by the action of urea on bovine β-lactoglobulins. Aust. J. Biol. Sci., 26, 859–70.
McKenzie, H.A., Ralston, G.B. and Shaw, D.C. (1972) Location of sulphydryl and disulphide groups in bovine β-lactoglobulins and effects of urea. Biochem., 11, 4539–47.
McKenzie, H.A. and Sawyer, W.H. (1967) Effect of pH on β-lactoglobulins. Nature, 214, 1101–4.
McKenzie, H.A. and Shaw, D.C. (1972) Alternative positions for the sulphydryl group in β-lactoglobulin: the significance for sulphydryl location in other proteins. Nature, 238, 147–9.
Mendieta, J., Folque, H. and Tauler, R. (1999) Two-phase induction of the nonnative α-helical form of β-lactoglobulin in the presence of trifluoroethanol. Biophys. J., 76, 451–7.
Mercier, J.C. and Vilotte, J.L. (1993) Structure and function of milk protein genes. J. Dairy Sci., 76, 3079–98.
Mepham, T.B., Gayer., Martin, P. and Mercier, J.C. (1992) Biosynthesis of milk protein. In Advanced Dairy Chemistry I. Proteins, 2nd edn, (P.F. Fox ed.) Elsevier, Amsterdam and New York, pp. 491–543.
Mercier, J.C, Gaye, P., Soulier, S., Hue-Delahaie, D. and Vilotte, J.L. (1985) Construction and identification of recombinant plasmids carrying cDNAs coding for ovine αs1-, αS2-, β-, K-casein and β-lactoglobulin. Nucleotide sequence of αs1-casein cDNA. Biochemie., 67, 959–71.
Mills, O.E. (1976) Effect of temperature on tryptophan fluorescence of β-lactoglobulin B. Biochim. Biophys. Acta, 434, 324–32.
Mills, O.E. and Creamer, L.K. (1975) Conformational changes of bovine β-lactoglobulin at low pH. Biochim. Biophys. Acta, 379, 618–26.
Miranda, G. and Pelissier, J.-P. (1983) Kinetic studies of in vivo digestion of bovine unheated skim-milk proteins in rat stomach. J. Dairy Res., 50, 27–36.
Mohammadzadeh-K., A., Feeney, R.E. and Smith, L.M. (1969) Hydrophobic binding of hydrocarbons by proteins. I. Relationship of hydrocarbon structure. Biochim. Biophys. Acta, 194, 246–55.
Molinari, H., Ragona, L., Varani, L., Musco, G., Consonni, R., Zetta, L. and Monaco, H.L. (1996) Partially folded structure of monomeric bovine β-lactoglobulin. FEBS Lett., 381, 237–43.
Monaco, H.L., Zanotti, G., Spadon, P., Bolognesi, M., Sawyer, L. and Eliopoulos, E.E. (1987) Crystal-structure of the trigonal form of bovine β-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol., 197, 695–706.
Monti, J.C., Mermoud, A.-F. and Jolies, P. (1989) Anti-bovine β-lactoglobulin antibodies react with a human lactoferrin fragment and bovine β-lactoglobulin present in human milk. Experientia, 45, 178–80.
Moreaux, V. and Birlouez-Aragon, I. (1997) Degradation of tryptophan in heated β-lactoglobulin-lactose mixtures is associated with intense Maillard reaction. J. Agric. Food Chem., 45, 1905–10.
Morgan, F., Leonil, J., Molle, D. and Bouhallab, S. (1997) Nonenzymatic lactosylation of bovine β-lactoglobulin under mild heat treatment leads to structural heterogeneity of the glycoforms. Biochem. Biophys. Res. Commun., 236, 413–7.
Morgan, F., Molle, D., Henry, G., Venien, A., Leonil, J., Peltre, G., Levieux, D., Maubois, J.L. and Bouhallab, S. (1999) Glycation of bovine β-lactoglobulin: effect on the protein structure. Int. J. Food Sci. Technol., 34, 429–35.
Mullally, M.M., Meisel, H. and Fitzgerald, R.J. (1996) Synthetic peptides corresponding to α-lactalbumin and β-lactoglobulin sequences with angiotensin-I-converting enzyme-inhibitory activity. Biol. Chem. Hoppe-Seyler, 377, 259–60.
Murray, B.S. and Cros, L. (1998) Adsorption of β-lactoglobulin and β-casein to metal surfaces and their removal by a non-ionic surfactant, as monitored via a quartz crystal microbalance. Colloid. Surfaces B, 10, 227–41.
Narayan, M. and Berliner, L.J. (1997) Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochem., 36, 1906–11.
Narayan, M. and Berliner, L.J. (1998) Mapping fatty acid binding to β-lactoglobulin: ligand binding is restricted by modification of Cys 121. Protein Sci., 7, 150–7.
Nath, N.C., Hussain, A. and Rahman, F. (1993) Milk characteristics of a captive Indian rhinoceros (Rhinoceros unicornis) J. Zoo Wildlife Med., 24, 528–33.
Neurath, A.R., Jiang, S.B., Strick, N., Lin, K., Li, Y.Y. and Debnath, A.K. (1996) Bovine β-lactoglobulin modified by 3-hydroxyphthalic anhydride blocks the CD4 cell-receptor for HIV. Nature Medicine, 2, 230–4.
Neuteboom, B., Giuffrida, M.G., Cantisani, A., Napolitano, L., Alessandri, A., Fabris, C, Bertino, E. and Conti, A. (1992) Human-milk components cross-reacting with antibodies against bovine β-lactoglobulin. Acta Paediatr., 81, 469–74.
Newcomer, M.E. (1993) Structure of the epididymal retinoic acid-binding protein at 2.1 A resolution. Structure, 1, 7–18.
Newcomer, M.E., Jones, T.A., Aqvist, J., Sundelin, J., Erikkson, U., Rask, L. and Peterson, P.A. (1984) The three dimensional structure of retinol-binding protein. EMBO J., 3, 1451–4.
North, A.C.T. (1989) 3-D arrangement of conserved amino acids in a superfamily of specific ligand-binding proteins. Int. J. Biol. Macromol., 7, 56–8.
North, A.C.T. (1991) Structural homology in ligand specific transport proteins. Biochem. Soc. Symp., 57, 35–48.
O’Neill, T.E. and Kinsella, J.E. (1987) Binding of alkanone flavors to β-lactoglobulin: effects of conformational and chemical modification. J. Agri. Food Chem., 35, 770–4.
Ochirkhuyag, B., Chobert, J.M., Dalgalarrondo, M., Choiset, Y. and Haertlé, T. (1998) Characterization of whey proteins from mongolian yak, khainak and bactrian camel. J. Food Biochem., 22, 105–24.
Ono, J., Doi, K., Ogasa, K. and Nagasawa, T. (1975) Discrimination of carcinogenic activity and inactivation of transforming activity of hydrocarbons by β-lactoglobulin. Agric. Biol. Chem., 39, 2149–55.
Otte, J.A.H.J., Kristiansen, K.R., Zakora, M. and Qvist, K.B. (1994) Separation of individual whey proteins and measurement of α-lactalbumin and β-lactoglobulin by capillary zone electrophoresis. Neth. Milk Dairy J., 48, 81–97.
Ouwehand, A.C., Salminen, S.J., Skurnik, M. and Conway, P.L. (1997) Inhibition of pathogen adhesion by β-lactoglobulin. Int. Dairy J., 7, 685–92.
Pace, N.C. and Tanford, C. (1968) Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55°C. Biochem., 7, 198–208.
Paesen, G.C., Adams, P.L., Harlos, K., Nuttall, P.A. and Stuart, D.I. (1999) Tick histamine-binding proteins: Isolation, cloning, and three-dimensional structure. Molecular Cell, 3, 661–71.
Palmer, A.H. (1934) The preparation of a crystalline globulin from the albumin fraction of cow’s milk. J. Biol. Chem., 104, 359–72.
Panick, G., Malessa, R. and 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. Biochem., 38, 6512–9.
Pantaloni, D. (1962) Role des groupes SH dans la structure de la β-lactoglobuline. Compt. Rend. Acad. Sci., (Paris)., 254, 1884–6.
Pantaloni, D. (1964) Etude de la transition R-S de la β-lactoglobuline par spectropolarimetrie et par spectrophotometrie de differences. Compt. Rend. Acad. Sci., (Paris)., 258, 5753–6.
Pantaloni, D. (1965) Structure et Changements de Conformations de la β-Lactoglobuline en Solution. Doctoral Thesis, University of Paris, France.
Papiz, M.Z., Sawyer, L., Eliopoulos, E.E., North, A.C.T., Findlay, J.B.C., Sivaprasadarao, R., Jones, T.A., Newcomer, M.E. and Kraulis, P.J. (1986) The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature, 324, 383–5.
Park, K.H. and Lund, D.B. (1984) Calorimetric study of the thermal denaturation of β-lactoglobulin. J. Dairy. Sci., 67, 1699–706.
Passey, R.J. and Mackinlay, A.G. (1995) Characterization of a second, apparently inactive, copy of the bovine β-lactoglobulin gene. Eur. J. Biochem., 233, 736–43.
Paterson, G.R., Otter, D.E. and Hill, J.P. (1995) Application of capillary electrophoresis in the identification of phenotypes containing the β-lactoglobulin-C variant. J. Dairy Sci., 78, 2637–44.
Peitsch, M.C. and Boguski, M.S. (1990) Is apolipoprotein D a mammalian bilinbinding protein? New Biologist, 2, 197–206.
Pelletier, E., Sostmann, K. and Guichard, E. (1998) Measurement of interactions between β-lactoglobulin and flavor compounds (esters, acids and pyrazines) by affinity and exclusion size chromatography. J. Agric. Food Chem., 46, 1506–9.
Pena, R.N., Sanchez, A., Coll, A. and Folch, J.M. (1999) Isolation, sequencing and relative quantitation by fluorescent-ratio PCR of feline β-lactoglobulin I, II and III cDNAs. Mammalian Genome, 10, 560–4.
Pérez, M.D. and Calvo, M. (1995) Interaction of β-lactoglobulin with retinol and fatty acids and its role as a possible biological function for this protein: a review. J. Dairy Sci., 78, 978–88.
Pérez, M.D., Devillegas, C.D., Sanchez, L., Aranda, P., Ena, J.M. and Calvo, M. (1989) Interaction of fatty-acids with β-lactoglobulin and albumin from ruminant milk. J. Biochem., 106, 1094–7.
Pérez, M.D., Sanchez, L., Aranda, P., Ena, J.M., Oria, R. and Calvo, M. (1992) Effect of β-lactoglobulin on the activity of pregastric lipase — a possible role for this protein in ruminant milk. Biochim. Biophys. Acta, 1123, 151–5.
Pérez-Gomez, G., Préaux, G. and Lontie, R. (1971) Location of the disulphide bridges in β-lactoglobulin B with pepsin and trypsin after CNBr cleavage. Arch. Int. Physiol. Biochim., 79, 843–4.
Pervaiz, S. and Brew, K. (1985) Homology of β-lactoglobulin, serum retinol-binding protein and protein HC. Science, 228, 335–7.
Pervaiz, S. and Brew, K. (1986) Purification and characterization of the major whey proteins from the milks of the bottlenose dolphin (Tursiops truncatus), the Florida manatee (Trichechus manatus latirostris) and the beagle (Canis familiaris). Arch. Biochem. Biophys., 246, 846–54.
Pervaiz, S. and Brew, K. (1987) Homology and structure-function correlations between α-1-acid glycoprotein and serum retinol-binding protein and its relatives. FASEB J., 1, 209–14.
Pessen, H., Purcell, J.M. and Farrell, H.M., Jr. (1985) Proton relaxation rates of water in dilute solutions of β-lactoglobulin: Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of a selfassociating globular protein. Biochim. Biophys. Acta, 828, 1–12.
Phelan, P. and Malthouse, J.P.G. (1994) C-13 NMR of the cyanylated β-lactoglobulins — evidence that Cys-121 provides the thiol group of β-lactoglobulins A and B. Biochem. J., 302, 511–6.
Pierce, A.E. (1960) β-Lactoglobulins in the urine of the new-born suckled calf. Nature, 186, 940–1.
Piez, K.A., Davie, E.W., Folk, J.E. and Gladner, J.A. (1961) β-Lactoglobulins A and B. J. Biol. Chem., 236, 2912–6.
Piotte, C.P., Hunter, A.K., Marshall, C.J. and Grigor, M.R. (1998) Phylogenetic analysis of three lipocalin-like proteins present in the milk of Trichosurus vulpecula (Phalangeridae, Marsupialid). J. Mol. Evol., 46, 361–9.
Pittia, P., Wilde, P.J., Husband, F. and Clark, D.C. (1996) Functional and structural properties of β-lactoglobulin as affected by high pressure treatment. J. Food Sci., 61, 1123–8.
Polis, P.D., Schmuckler, H.W., Custer, J.H. and McMeekin, T.L. (1950) Isolation of an electrophoretically homogeneous crystalline component of β-lactoglobulin. J. Amer. Chem. Soc., 72, 4965–8.
Préa ux, G., Braunitzer, G., Schrank, B. and Stangl, A. (1979) The amino acid sequence of goat β-lactoglobulin. Hoppe Seyler’s Z. Physiol. Chem., 360, 1595–604.
Préaux, G. and Lontie, R. (1972) Revised number of the free cysteine residues and of the disulphide bridges in the sequence of β-lactoglobulins A and B. Arch. Int. Physiol. Biochim., 80, 980–1.
Presnell, B., Conti, A., Erhardt, G., Krause, I. and Godovac-Zimmermann, J. (1990) A rapid microbore HPLC method for determination of primary structure of β-lactoglobulin genetic-variants. J. Biochem. Biophys. Meth., 20, 325–33.
Prinzenberg, E.M. and Erhardt, G. (1999) Molecular genetic characterization of ovine β-lactoglobulin C allele and detection by PCR-rflp. J. Anim. Breeding Gen. Z. Tier. Zuch., 116, 9–14.
Prutz, W.A., Butler, J., Land, E.J. and Swallow, A.J. (1980) Direct demonstration of electron transfer between tryptophan and tyrosine in proteins. Biochem. Biophys. Res. Commun., 96, 408–14.
Purcell, J.M. and Susi, H. (1984) Solvent denaturation of proteins as observed by resolution-enhanced Fourier transform infrared spectroscopy. J. Biochem. Biophys. Meth., 9, 193–9.
Puyol, P., Pérez, M.D., Ena, J.M. and Calvo, M. (1991) Interaction of bovine β-lactoglobulin and other bovine and human whey proteins with retinol and fatty/ acids. Agric. Biol. Chem., 55, 2515–20.
Puyol, P., Pérez, M.D., Peiro, J.M. and Calvo, M. (1994) Effect of binding of retinol and palmitic acid to bovine β-lactoglobulin on its resistance to thermal denaturation. J. Dairy Sci., 77, 1494–502.
Puyol, P., Pérez, M.D., Sanchez, L., Ena, J.M. and Calvo, M. (1995) Uptake and passage of β-lactoglobulin, palmitic acid and retinol across the caco-2 monolayer. Biochim. Biophys. Acta, 1236, 149–54.
Qi, X.L., Brownlow, S., Holt, C. and Sellers, P. (1995) Thermal-denaturation of β-lactoglobulin — effect of protein-concentration at pH 6.75 and pH 8.05. Biochim. Biophys. Acta, 1248, 43–9.
Qi, X.L., Holt, C, McNulty, D., Clarke, D.T., Brownlow, S. and Jones, G.R. (1997) 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. Biochem. J., 324, 341–6.
Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N., a.:d Jameson G.B. (1999) Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Prot. Sci., 8, 75–83.
Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.M., Baker, E.N. and Jameson, G.B. (1998a) Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochem., 37, 14014–23.
Qin, B.Y., Creamer, L.K., Baker, E.N. and Jameson, G.B. (1998b) 12-Bromododecanoic acid binds inside the calyx of bovine β-lactoglobulin. FEBS Lett., 438, 272–8.
Ragona, L., Fogolari, F., Romagnoli, S., Zetta, L., Maubois, J.L. and Molinari, H. (1999) Unfolding and refolding of bovine β-lactoglobulin monitored by hydrogen exchange measurements. J. Mol. Biol., 293, 953–69.
Ragona, L., Fogolari, F., Zetta, L., Pérez, M.D., Puyol, P., de Kruif, K., Löhr, F., Röterjans, H. and Molinari, H. (2000) Bovine β-lactoglobulin: interaction studies with palmitic acid. Protein Science, 9, 1347–56.
Ragona, L., Pusteria, F., Zetta, L., Monaco, H.L. and Molinari, H. (1997) Identification of a conserved hydrophobic cluster in partially folded bovine β-lactoglobulin at pH 2. Folding Design, 2, 281–90.
Ray, A. and Chatterjee, R. (1967) Interactions of β-lactoglobulins with large organic ions. In Conformation of Biopolymers, Vol. 1. (G.N. Ramachandran ed.) Academic Press, London, pp. 235–52.
Relkin, P. (1996) Thermal unfolding of β-lactoglobulin, α-lactalbumin and bovine serumlbumin — a thermodynamic approach. Crit. Rev. Food Sci. Nutr., 36, 565–601.
Renard, D., Lefebvre, J., Griffin, M.C.A. and Griffin, W.G. (1998) Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies. Int. J. Biol. Macromol., 22, 41–9.
Restani, P., Gaiaschi, A., Plebani, A., Beretta, B., Cavagni, G., Fiocchi, A., Poiesi, C, Velona, T., Ugazio, A.G. and Galli, C.L. (1999) Cross-reactivity between milk proteins from different animal species. Clin. Exptl. Allergy, 29, 997–1004.
Richards, F.M. (1991) The protein folding problem. Scientific American, 264, 54–62.
Robillard, K.A. and Wishnia, A. (1972) Hydrophobic interactions between small molecules and β-lactoglobulin A. Aromatic hydrophobes and β-lactoglobulin A. Kinetics of binding by nuclear magnetic resonance. Biochemistry, 11, 3841–5.
Rocha, T.L., Brownlow, S., Saddler, K.N., Fothergill-Gilmore, L.A. and Sawyer, L. (1996a) New crystal form of β-lactoglobulin. J. Dairy Res., 63, 575–84.
Rocha, T.L., Paterson, G., Crimmins, K., Boyd, A., Sawyer, L. and Fothergill-Gilmore, L.A. (1996b) Expression and secretion of recombinant ovine β-lactoglobulin in Saccharomyces cerevisiae and Kluyveromyces lactis. Biochem. J., 313, 927–32.
Roefs, S.P.F.M. and de Kruif, K.G. (1994) A model for the denaturation and aggregation of β-lactoglobulin. Eur. J. Biochem., 226, 883–9.
Roels, H., Préaux, G. and Lontie, R. (1966) Stabilization of β-lactoglobulin A and B at pH 8.9 by blocking the thiol groups. Arch. Int. Biochem., 74, 522–3.
Roscoe, S.G. and Fuller, K.L. (1993) Fouling of model surfaces — adsorption and removal of K-casein and β-lactoglobulin. Food Res. Int., 26, 343–53.
Rouhana, R., Budge, S.M., Macdonald, S.M. and Roscoe, S.G. (1997) Electrochemical studies of the interfacial behaviour of α-lactalbumin and bovine serum albumin. Food Res. Int., 30, 13–20.
Rouvinen, J., Rautiainen, J., Virtanen, T., Zeiler, T., Kauppinen, J., Taivainen, A. and Mantyjarvi, R. (1999) Probing the molecular basis of allergy — threedimensional structure of the bovine lipocalin allergen Bos-d2. J. Biol. Chem., 274, 2337–43.
Rüegg, M., Moor, U. and Blanc, B. (1975) Hydration and thermal denaturation of β-lactoglobulin. A calorimetric study. Biochim. Biophys. Acta, 400, 334–42.
Said, H.M., Ong, D.E. and Shingleton, J.L. (1989) Intestinal uptake of retinol, enhancement by bovine milk β-lactoglobulin. Amer. J. Clin. Nutr., 49, 690–4.
Sawyer, L. (1987) One fold among many. Nature, 327, 659 (1 page).
Sawyer, L. and Green, D.W. (1979) The reaction of cow β-lactoglobulin with tetracyanoaurate(III). Biochim. Biophys. Acta, 579, 234–9.
Sawyer, L. and James, M.N.G. (1982) Carboxyl-carboxylate interactions in proteins. Nature, 295, 79–80.
Sawyer, L., Brownlow, S., Polikarpov, I. and Wu, S.Y. (1998) β-Lactoglobulin: structural studies, biological clues. Int. Dairy J., 8, 65–72.
Sawyer, L., Papiz, M.Z., North, A.C.T. and Eliopoulos, E.E. (1985) Structure and function of bovine β-lactoglobulin. Biochem. Soc. Trans., 13, 265–6.
Sawyer, L., Barlow, P.N., Boland, M.J., Creamer, L.K., Denton, H., Edwards, P.J.B., Holt, C, Jameson, G.B., Kontopidis, G., Norris, G.E., Uhrinov, S. and Wu, S.-Y. (2002) Milk protein structure—what can it tell the diary industry? Int. Dairy J., 12, 299–310.
Sawyer, W.H. (1969) Complex between β-lactoglobulin and K-casein. A review. J. Dairy Sci., 52, 1347–55.
Schlee, P., Krause, I. and Rottmann, O. (1993) Genotyping of ovine β-lactoglobulin alleles A and B using the polymerase chain-reaction. Archiv. Für Tierzucht., 36, 519–23.
Seibles, T.S. (1969) Interaction of dodecyl sulphate with native and modified β-lactoglobulin. Biochemistry, 8, 2949–54.
Sélo, I., Negroni, L., Creminon, C, Yvon, M., Peltre, G. and Wal, J.M. (1998) Allergy to bovine β-lactoglobulin: specificity of human IgE using cyanogen bromide-derived peptides. Int. Arch. Allergy Immunol., 117, 20–8.
Senti, F.R. and Warner, R.C. (1948) X-Ray molecular weight of β-lactoglobulin. J. Amer. Chem. Soc., 70, 3318–20.
Seppala, M., Bohn, H. and Tatarinov, Y. (1998) Glycodelins. Tumor Biology, 19, 213–20.
Shimoyamada, M., Yoshimura, H., Tomida, K. and Watanabe, K. (1996) Stabilities of bovine β-lactoglobulin/retinol or retinoic acid complexes against tryptic hydrolysis, heating and light-induced oxidation. Food Sci. Technol.-Lebens. Wiss. Technol., 29, 763–6.
Shortle, D., Stites, W.E. and Meeker, A.K. (1990) Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochem., 29, 8033–41.
Simons, J.P., McClenaghan, M. and Clark, AJ. (1987) Alteration of the quality of milk by expression of sheep β-lactoglobulin in transgenic mice. Nature, 328, 530–2.
Sitohy, M., Chobert, J.M. and Haertlé, T. (1995a) Phosphorylation of β-lactoglobulin using amino-acids as the sole base and nucleophile of the reaction. J. Prot. Chem., 14, 145–50.
Sitohy, M., Chobert, J.M. and Haertlé, T. (1995b) Amino acid grafting of β-lactoglobulin mediated by phosphorus oxychloride. Int. J. Biol. Macromol., 17, 269–72.
Smith, L.M., Fantozzi, P. and Creveling, R.K. (1983) Study of triglyceride-protein interaction using a microemulsion-filtration method. J. Amer. Oil Chem. Soc., 60, 960–7.
Sorva, R., Makinen-Kiljunen, S. and Juntunen-Backman, K. (1994) β-Lactoglobulin secretion in human milk varies widely after cows milk ingestion in mothers of infants with cows’ milk allergy. J. Allergy Clin. Immunol., 93, 787–92.
Spector, A.A. and Fletcher, J.E. (1970) Binding of long chain fatty acids to β-lactoglobulin. Lipids, 5, 403–11.
Stapelfeldt, H., Olsen, C.E. and Skibsted, L.H. (1999) Spectrofluorometric characterization of β-lactoglobulin B covalently labeled with 2-(4′-maleimidylanilino) naphthalene-6-sulfonate. J. Agric. Food Chem., 47, 3986–90.
Steinrauf, L.K. (1959) Preliminary X-ray data for some new crystalline forms of β-lactoglobulin and hen egg-white lysozyme. Acta Cryst., 12, 77–9.
Stone, W.L. and Wishnia, A. (1978) Binding of iodomercurates to sulphydryl-blocked β-lactoglobulin-A,-B and-C. Bioinorg. Chem., 8, 517–29.
Strange, E.D., Malin, E.L. and Vanhekken, D.L. (1992) Chromatographic and electrophoretic methods used for analysis of milk-proteins. J. Chromatogr., 624, 81–102.
Su, Y.T. and Jirgensons, B. (1977) Further studies on detergent-induced conformational transitions in proteins. Circular dichroism of ovalbumin, bacterial α-amylase, papain and β-lactoglobulin at various pH values. Arch. Biochem. Biophys., 181, 137–46.
Subirade, M., Loupil, F., Allain, A.F. and Paquin, P. (1998) Effect of dynamic high pressure on the secondary structure of β-lactoglobulin and on its conformational properties as determined by fourier transform infrared spectroscopy. Int. Dairy J., 8, 135–40.
Subramaniam, V., Gafni, A. and Steel, D. (1996) Restoration of biological function upon refolding does not ensure return of a proteins native structure — room temperature phosphorescence studies of bovine β-lactoglobulin. Prot. Sci., 5, 2089–94.
Sugai, S., Ikeguchi, M. and Shimizu, A. (1999) Characteristic properties of equine milk proteins. Int. J. Food Sci. Technol., 34, 437–43.
Suzuki, S., Koritz, T.N. and Coomb, R.R.A. (1987) Antigenic stimulation with proteins of cows’ milk via the oral route in guinea-pigs and rats. 2. Antibodies to β-lactoglobulin secreted into the alimentary canal and serum. Int. Arch. All. Appl. Immun., 82, 76–82.
Svedberg, T. and Pedersen, K.O. (1940) The Ultracentrifuge. Oxford University Press, London.
Swaisgood, H.E. (1982) Chemistry of milk proteins. In Developments in Dairy Chemistry, (P.F. Fox ed.) Applied Science Publishers, London, pp. 1–59.
Takahashi, T., Yamauchi, K. and Kaminogawa, S. (1990) Comparison between the antigenicity of native and unfolded β-lactoglobulin. Agric. Biol. Chem., 54, 691–7.
Tanford, C, Bunville, L.G. and Nozaki, Y. (1959) The reversible transformation of β-lactoglobulin at pH 7.5. J. Amer. Chem. Soc., 81, 4032–6.
Tanford, C. and De, P.K. (1961) The unfolding of β-lactoglobulin at pH 3 by urea, formamide and other organic substances. J. Biol. Chem., 236, 1711–5.
Tanford, C. and Taggart, V.G. (1961) Ionization-linked changes in protein conformation, II. The N-R transition in β-lactoglobulin. J. Amer. Chem. Soc., 83, 1634–8.
Tedford, L.A., Kelly, S.M., Price, N.C. and Schaschke, C.J. (1999) Interactive effects of pressure, temperature and time on the molecular structure of β-lactoglobulin. J. Food Sci., 64, 396–9.
Tegoni, M., Ramoni, R., Bignetti, E., Spinelli, S. and Cambillau, C. (1996) Domain swapping creates a third putative combining site in bovine odorant binding protein dimer. Nature Struct. Biol., 3, 863–7.
Thompson, M.P. and Farrell, H.M., Jr. (1974) Genetic variants of milk proteins. In Lactation: A Comprehensive Treatise. Vol. III. (B.L. Larson and V.R. Smith eds.) Academic Press, New York, pp. 109–34.
Thresher, W. and Hill, J.P. (1997) Thermodynamic characterisation of β-lactoglobulin A, B and C subunit interactions using analytical affinity chromatography. In Milk Protein Polymorphism, (J.P. Hill and M. Boland eds.) Special Issue, 9702, International Dairy Federation, Brussels, pp. 189–93.
Tilley, J.M.A. (1960) The chemical and physical properties of bovine β-lactoglobulin. Dairy. Sci. Abstr., 22, 111–25.
Timasheff, S.N., Mescanti, L., Basch, J.J. and Townend, R. (1966a) Conformational transitions of bovine β-lactoglobulins A, B and C. J. Biol. Chem., 241, 2496–501.
Timasheff, S.N. and Susi, H. (1966) Infrared investigation of the secondary structure of β-lactoglobulins. J. Biol. Chem., 241, 249–51.
Timasheff, S.N. and Townend, R. (1961) Molecular interactions in β-lactoglobulin. V. The association of the genetic species of β-lactoglobulin below the isoelectric point. J. Amer. Chem. Soc., 83, 464–9.
Timasheff, S.N. and Townend, R. (1964) Structure of the β-lactoglobulin tetramer. Nature, 203, 517–9.
Timasheff, S.N., Townend, R. and Mescanti, L. (1966b) The optical rotatory dispersion of β-lactoglobulins. J. Biol. Chem., 241, 1863–70.
Townend, R., Herskovits, T.T., Timasheff, S.N. and Gorbunoff, M.J. (1969) The state of amino acid residues in β-lactoglobulin. Arch. Biochem. Biophys., 129, 567–80.
Townend, R., Kumosinski, T.F. and Timasheff, S.N. (1967) The circular dichroism of variants of β-lactoglobulin. J. Biol. Chem., 242, 4538–45.
Townend, R. and Timasheff, S.N. (1960) Molecular interactions in β-lactoglobulin. III. Light scattering investigation of the stoichiometry of the association between pH 3.7 and 5.2. J. Amer. Chem. Soc., 82, 3168–74.
Townend, R., Weinberger, L. and Timasheff, S.N. (1960b) Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5. J. Amer. Chem. Soc., 82, 3175–9.
Townend, R., Winterbottom, R.J. and Timasheff, S.N. (1960a) Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point. J. Amer. Chem. Soc., 82, 3161–8.
Treece, J.M., Sheinson, R.S. and McMeekin, T.L. (1964) The solubilities of β-lactoglobulins A, B and AB. Arch. Biochem. Biophys., 108, 99–108.
Tsuji, N.M., Kurisaki, J., Mizumachi, K. and Kaminogawa, S. (1993) Localization of T-cell determinants on bovine β-lactoglobulin. Immunol. Lett., 37, 215–21.
Uhrinova, S., Smith, M.H., Jameson, G.B., Uhrin, D., Sawyer, L. and Barlow, P.N. (2000) Structural changes accompanying pH-induced dissociation of the β-lactoglobulin dimer. Biochem., 39, 1113–23.
Urade, Y. and Hayaishi, O. (2000) Prostaglandin D synthase: structure and function. Vitamins and Hormones — Adv. Res. Appl., 58, 89–120.
ValenteMesquita, V.L., Botelho, M.M. and Ferreira, S.T. (1998) Pressure-induced subunit dissociation and unfolding of dimeric β-lactoglobulin. Biophys. J., 75, 471–6.
Venien, A., Levieux, D., Astier, C, Briand, L., Chobert, J.M. and Haertlé, T. (1997) Production and epitopic characterization of monoclonal antibodies against bovine β-lactoglobulin. J. Dairy Sci., 80, 1977–87.
Verheul, M., Pedersen, J.S., Roefs, S.P.F.M. and deKruif, K.G. (1999) Association behaviour of native β-lactoglobulin. Biopolymers, 49, 11–20.
Waissbluth, M.D. and Grieger, R.A. (1973) Activation volumes of fast protein reactions: the binding of bromophenol blue to β-lactoglobulin. Arch. Biochem. Biophys., 159, 639–45.
Wang, Q.W., Alien, J.C. and Swaisgood, H.E. (1997) Binding of vitamin D and cholesterol to β-lactoglobulin. J. Dairy Sci., 80, 1054–9.
Wang, Q.W. and Swaisgood, H.E. (1993) Characteristics of β-lactoglobulin binding to the all-trans-retinal moiety covalently immobilized on Celite. J. Dairy Sci., 76, 1895–901.
Wang, Q.W.Q., Alien, J.C. and Swaisgood, H.E. (1998) Protein concentration dependence of palmitate binding to β-lactoglobulin. J. Dairy Sci., 81, 76–81.
Waninge, R., Paulsson, M., Nylander, T., Ninham, B. and Sellers, P. (1998) Binding of sodium dodecyl sulphate and dodecyl trimethyl ammonium chloride to β-lactoglobulin: a calorimetric study. Int. Dairy., 8, 141–8.
Weichsel, A., Andersen, J.F., Champagne, D.E., Walker, F.A. and Montfort, W.R. (1998) Crystal structures of a nitric oxide transport protein from a blood-sucking insect. Nature Struct. Biol., 5, 304–9.
Weissman, J.S. and Kim, P.S. (1993) Efficient catalysis of disulfide bond rearrangements by protein disulfide-isomerase. Nature, 365, 185–8.
Westphal, U. and Ashley, B.D. (1958) Steroid-protein interactions: 4. Influence of functional groups in delta 4-3-ketosteroids on interaction with serum albumin and β-lactoglobulin. J. Biol. Chem., 233, 57–62.
Whitelaw, B. (1999) Toward designer milk. Nature Biotechnol., 17, 135–6.
Whitelaw, C.B.A., Harris, S., McClenaghan, M., Simons, J.P. and Clark, A.J. (1992) Position-independent expression of the ovine β-lactoglobulin gene in transgenic mice. Biochem. J., 286, 31–9.
Williams, S.C., Badley, R.A., Davis, P.J., Puijk, W.C. and Meloen, R.H. (1998) Identification of epitopes within β-lactoglobulin recognised by polyclonal antibodies using phage display and pepscan. J. Immunol. Meth., 213, 1–17.
Willis, I.M., Stewart, A.F., Caputo, A., Thompson, A.R. and Mackinlay, A.G. (1982) Construction and identification by partial nucleotide sequence analysis of bovine casein and β-lactoglobulin cDNA clones. DNA, 1, 375–86.
Wishnia, A. and Pinder, T.W., Jr. (1966) Hydrophobie interactions in proteins. The alkane binding site of β-lactoglobulins A and B. Biochem., 5, 1534–42.
Witz, J., Timasheff, S.N. and Luzzati, V. (1964) Molecular interaction in β-lactoglobulin. VIII Small-angle X-ray scattering investigation of the geometry of β-lactoglobulin A tetramerisation. J. Amer. Chem. Soc., 86, 168–73.
Woo, S.L., Creamer, L.K. and Richardson, T. (1982) Chemical phosphorylation of bovine β-lactoglobulin. J. Agri. Food Chem., 30, 65–70.
Woodlee, G.L., Gooley, A.A., Collet, C. and Cooper, D.W. (1993) Origin of late lactation protein from β-lactoglobulin in the tammar wallaby. J. Heredity, 84, 460–5.
Workman, R.J., McKown, M.M. and Gregerman, R.I. (1974) Renin: inhibition by proteins and peptides. Biochem., 13, 3029–35.
Wright, G., Carver, A., Cottom, D., Reeves, D., Scott, A., Simons, P., Wilmut, I., Garner, I. and Colman, A. (1991) High-level expression of active human α-1-antitrypsin in the milk of transgenic sheep. Bio-Technol., 9, 830–4.
Wu, S.Y., Pérez, M.D., Puyol, P. and Sawyer, L. (1999) β-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem., 274, 170–4.
Yoshida, S., Ye-Xiuyun, and Nishiumi, T. (1991) The binding ability of α-lactalbumin and β-lactoglobulin to mutagenic heterocyclic amines. J. Dairy Sci., 74, 3741–5.
Zanotti, G., Panzalorto, M., Marcato, A., Malpeli, G., Folli, C. and Berni, R. (1998) Structure of pig plasma retinol-binding protein at 1.65 Å resolution. Acta Cryst., D54, 1049–52.
Zappacosta, F., Diluccia, A., Ledda, L. and Addeo, F. (1998) Identification of C-terminally truncated forms of β-lactoglobulin in whey from Romagnola cows’ milk by two dimensional electrophoresis coupled to mass spectrometry. J. Dairy Res., 65, 243–52.
Zimmerman, J.K., Barlow, G.H. and Klotz, I.M. (1970) Dissociation of β-lactoglobulin near neutral pH. Arch. Biochem. Biophys., 138, 101–9.
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Sawyer, L. (2003). β-Lactoglobulin. In: Fox, P.F., McSweeney, P.L.H. (eds) Advanced Dairy Chemistry—1 Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-8602-3_7
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