Abstract
The whey protein β-lactoglobulin (β-Lg), a lipocalin, is widely distributed amongst mammals and is a small soluble protein found both as monomers and dimers, the latter being predominant in ruminant milks. β-Lg binds a wide variety of small, generally hydrophobic, molecules at a major internal binding site, although external sites have also been identified. The bovine protein undergoes several conformational changes and has a free sulphydryl group that appears to be responsible for polymerisation through disulphide interchange on heating. The biochemical properties of β-Lg are discussed with reference to the enormous literature that has been published over the last 75 years.
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Adams, J.J., Anderson, B.F., Norris, G.E., Creamer, L.K. and Jameson, G.B. (2006). Structure of bovine β-lactoglobulin (variant A) at very low ionic strength. J. Struct. Biol. 154, 246–254.
Åkerström, B., Borregaard, N., Flower, D.R. and Salier, J.-P. (2006). Lipocalins. Landes Bioscience, Georgetown.
Alexander, L.J. and Pace, C.N. (1971). A comparison of the denaturation of bovine β-lactoglobulins A and B and goat β-lactoglobulin. Biochemistry 10, 2738–2743.
Alexander, L.J., Hayes, G., Pearse, M.J., Beattie, C.W., Stewart, A.F., Willis, I.M. and Mackinlay, A.G. (1989). Complete sequence of the bovine β-lactoglobulin cDNA. Nucleic Acids Res. 17, 6739.
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. Biol. 199, 415–426.
Ando, K., Mori, M., Kato, I., Yuas, K. and Goda, K. (1979). General composition and chemical properties of the main components of Yezo brown bear (Ursus arctos yesonensis) milks. J. College Dairying (Ehetsu) 8, 9–21.
Aoki, T., Iskandar, S., Yoshida, T., Takahashi, K. and Hattori, M. (2006). Reduced immunogenicity of β-lactoglobulin by conjugating with chitosan. Biosci. Biotech. Bioch. 70, 2349–2356.
Aouzelleg, A., Bull, L.A., Price, N.C. and Kelly, S.M. (2004). Molecular studies of pressure/temperature-induced structural changes in bovine β-lactoglobulin. J. Sci. Food Agr. 84, 398–404.
Arai, M., Ikura, T., Semisotnov, G.V., Kihara, H., Amemiya, Y. and Kuwajima, K. (1998). Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. J. Mol. Biol. 275, 149–162.
Arakawa, T. and Timasheff, S.N. (1987). Abnormal solubility behaviour of β-lactoglobulin: salting-in by glycine and NaCl. Biochemistry 26, 5147–5153.
Arakawa, T., Kita, Y. and Timasheff, S.N. (2007). Protein precipitation and denaturation by dimethyl sulfoxide. Biophys. Chem. 131, 62–70.
Ariyaratne, K.A.N.S., Brown, R., Dasgupta, A., de Jonge, J., Jameson, G.B., Loo, T.S., Weinberg, C. and Norris, G.E. (2002). Expression of bovine β-lactoglobulin as a fusion protein in Escherichia coli: a tool for investigating how structure affects function. Int. Dairy J. 12, 311–318.
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. Acta 147, 93–99.
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.
Arnoux, P., Morosinotto, T., Saga, G., Bassi, R. and Pignol, D. (2009). A structural basis for the pH-dependent xanthophyll cycle in Arabidopsis thaliana. Plant Cell 21, 2036–2044.
Aschaffenburg, R. and Drewry, J. (1955). Occurrence of different β-lactoglobulins in cow’s milk. Nature 176, 218–219.
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, 273–277.
Aschaffenburg, R., Green, D.W. and Simmons, R.M. (1965). Crystal forms of β-lactoglobulin. J. Mol. Biol. 13, 194–201.
Attwood, T.K., Bradley, P., Flower, D.R., Gaulton, A., Maudling, N., Mitchell, A., Moulton, G., Nordle, A., Paine, K., Taylor, P., Uddin, A. and Zygouri, C. (2003). PRINTS and its automatic supplement, prePRINTS. Nucleic Acids Res. 31, 400–402.
Axelsson, I., Jakobsson, I., Lindberg, T. and Benediktsson, B. (1986). Bovine β-lactoglobulin in the human milk—a longitudinal-study during the whole lactation period. Acta Paediatr. Scand. 75, 702–707.
Aymard, P., Durand, D. and Nicolai, T. (1996). The effect of temperature and ionic-strength on the dimerization of β-lactoglobulin. Int. J .Biol. Macromol. 19, 213–221.
Azuma, N. and Yamauchi, K. (1991). Identification of α-lactalbumin and β-lactoglobulin in cynomolgus monkey (Macaca fascicularis) milk. Comp. Biochem. Phys. B 99, 917–921.
Bain, J.A. and Deutsch, H.F. (1948). Studies on lactoglobulins. Arch. Biochem. Biophys. 16, 221–229.
Ballester, M., Sanchez, A. and Folch, J.M. (2005). Polymorphisms in the goat β-lactoglobulin gene. J. Dairy Res. 72, 379–384.
Bansal, B. and Chen, X.D. (2006). A critical review of milk fouling in heat exchangers. Compr. Rev. Food Sci. F 5, 27–33.
Bao, Z.J., Wang, S.J., Shi, W., Dong, S. and Ma, H. (2007). Selective modification of Trp19 in β-lactoglobulin by a new diazo fluorescence probe. J. Proteome Res. 6, 3835–3841.
Batt, C.A., Rabson, L.D., Wong, D.W.S. and Kinsella, J.E. (1990). Expression of recombinant bovine β-lactoglobulin in Escherichia coli. Agric. Biol. Chem. 54, 949–955.
Batt, C.A., Brady, J. and Sawyer, L. (1994). Design improvements of β-lactoglobulin. Trends Food Sci. Tech. 5, 261–265.
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.
Bell, K. and McKenzie, H.A. (1964). β-Lactoglobulins. Nature 204, 1275–1279.
Bell, K. and McKenzie, H.A. (1967). The isolation and properties of bovine β-lactoglobulin C. Biochim. Biophys. Acta 147, 109–122.
Bell, K., McKenzie, H.A. and Shaw, D.C. (1981a). Porcine β-lactoglobulin A and C. Mol. Cell. Biochem. 35, 103–111.
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, 133–147.
Bell, K., McKenzie, H.A., Muller, V., Rogers, C. and Shaw, D.C. (1981c). Equine whey proteins. Comp. Biochem. Phys. B 68, 225–236.
Bello, M., Perez-Hernandez, G., Fernandez-Velasco, D.A., Arreguin-Espinosa, R. and Garcia-Hernandez, E. (2008). Energetics of protein homodimerization: effects of water sequestering on the formation of β-lactoglobulin dimer. Proteins 70, 1475–1487.
Bello, M., Portillo-Tellez, M.D. and Garcia-Hernandez, E. (2011). Energetics of ligand recognition and self-association of bovine β-lactoglobulin: differences between variants A and B. Biochemistry 50, 151–161.
Belloque, J. and Smith, G.M. (1998). Thermal denaturation of β-lactoglobulin. A H-1 NMR study. J. Agric. Food Chem. 46, 1805–1813.
Belloque, J., Lopez-Fandino, R. and Smith, G.M. (2000). A H-1-NMR study on the effect of high pressures on β-lactoglobulin. J. Agric. Food Chem. 48, 3906–3912.
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, 543–549.
Bertonati, C., Honig, B. and Alexov, E. (2007). Poisson-Boltzmann calculations of nonspecific salt effects on protein-protein binding free energies. Biophys. J. 92, 1891–1899.
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. U S A 96, 1898–1903.
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., International Dairy Federation, Brussels. pp. 100–109.
Bhattacharjee, C., Saha, S., Biswas, A., Kundu, M., Ghosh, L. and Das, K.P. (2005). Structural changes of β-lactoglobulin during thermal unfolding and refolding—an FT-IR and circular dichroism study. Protein J. 24, 27–35.
Bohr, H. and Bohr, J. (2000). Microwave-enhanced folding and denaturation of globular proteins. Phys. Rev. E. Part B 61, 4310–4314.
Boye, J.I., Ma, C.Y. and Ismail, A. (2004). Thermal stability of β-lactoglobulins A and B: effect of SDS, urea, cysteine and N-ethylmaleimide. J. Dairy Res. 71, 207–215.
Brans, G., Schroen, C.G.P.H., van der Sman, R.G.M. and Boom, R.M. (2004). Membrane fractionation of milk: state of the art and challenges. J. Membrane. Sci. 243, 263–272.
Braunitzer, G., Chen, R., Schrank, B. and Stangl, A. (1972). Automatische Sequenzanalyse eines Proteins (β-Lactoglobulin AB). Hoppe-Seyler’s Z. Physiol. Chem. 353, 832–834.
Braunschweig, M.H. (2007). Duplication in the 5′-flanking region of the β-lactoglobulin gene is linked to the BLG A allele. J. Dairy Sci. 90, 5780–5783.
Breustedt, D.A., Korndorfer, I.P., Redl, B. and Skerra, A. (2005). The 1.8Å crystal structure of human tear lipocalin reveals an extended branched cavity with capacity for multiple ligands. J. Biol. Chem. 280, 484–493.
Brew, K. and Campbell, P.N. (1967). The characterization of the whey proteins of guinea-pig milk. Biochem. J. 102, 258–264.
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, 156–164.
Brownlow, S., Cabral, 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, 481–495.
Buetler, T.M., Leclerc, E., Baumeyer, A., Latado, H., Newell, J., Adolfsson, O., Parisod, V., Richoz, J., Maurer, S., Foata, F., Piguet, D., Junod, S., Heizmann, C.W. and Delatour, T. (2008). N-ε-Carboxymethyllysine-modified proteins are unable to bind to RAGE and activate an inflammatory response. Mol. Nutr. Food Res. 52, 370–378.
Bull, H.B. and Currie, B.T. (1946). Osmotic pressure of β-lactoglobulin solutions. J. Am. Chem. Soc. 68, 742–748.
Burova, T.V., Choiset, Y., Tran, V. and Haertlé, T. (1998). Role of free Cys121 in stabilization of bovine β-lactoglobulin B. Protein Eng. 11, 1065–1073.
Burova, T.V., Grinberg, N.V., Visschers, R.W., Grinberg, V.Y. and de Kruif, C.G. (2002). Thermodynamic stability of porcine β-lactoglobulin—a structural relevance. Eur. J. Biochem. 269, 3958–3968.
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, 143–148.
Busti, P., Scarpeci, S., Gatti, C.A. and Delorenzi, N.J. (2005). Binding of alkylsulfonate ligands to bovine β-lactoglobulin: effects on protein denaturation by urea. Food Hydrocoll. 19, 249–255.
Caillard, R., Boutin, Y. and Subirade, M. (2011). Characterization of succinylated β-lactoglobulin and its application as the excipient in novel delayed release tablets. Int. Dairy J. 21, 27–33.
Cane, K.N., Arnould, J.P.Y. and Nicholas, K.R. (2005). Characterisation of proteins in the milk of fur seals. Comp. Biochem. Physiol. B 141, 111–120.
Caroli, A.M., Chessa, S. and Erhardt, G.J. (2009). Invited review: Milk protein polymorphisms in cattle: effect on animal breeding and human nutrition. J. Dairy Sci. 92, 5335–5352.
Carrotta, R., Arleth, L., Pedersen, J.S. and Bauer, R. (2003). Small-angle X-ray scattering studies of metastable intermediates of β-lactoglobulin isolated after heat-induced aggregation. Biopolymers 70, 377–390.
Casal, H.L., Kohler, U. and Mantsch, H.N. (1988). Structural and conformational 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, 33–35.
Chakraborty, J., Das, N., Das, K.P. and Halder, U.C. (2009). Loss of structural integrity and hydrophobic ligand binding capacity of acetylated and succinylated bovine β-lactoglobulin. Int. Dairy. J. 19, 43–49.
Chamani, J. (2006). Comparison of the conformational stability of the non-native α-helical intermediate of thiol-modified β-lactoglobulin upon interaction with sodium n-alkyl sulfates at two different pH. J. Colloid Interf. Sci. 299, 636–646
Chaneton, L., Saez, J.M.P. and Bussmann, L.E. (2011). Antimicrobial activity of bovine β-lactoglobulin against mastitis-causing bacteria. J. Dairy Sci. 94, 138–145.
Changani, S.D., Belmar-Beiny, M.T. and Fryer, P.J. (1997). Engineering and chemical factors associated with fouling and cleaning in milk processing. Exp. 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, 1113–1118.
Chessa, S., Chiatti, F., Ceriotti, G., Caroli, A., Consolandi, C., Pagnacco, G. and Castiglioni, B. (2007). Development of a single nucleotide polymorphism genotyping microarray platform for the identification of bovine milk protein genetic polymorphisms. J. Dairy Sci. 90, 451–464.
Chiancone, E. and Gattoni, M. (1993). Selective removal of β-lactoglobulin directly from cow’s milk and preparation of hypoallergenic formulas—a bioaffinity method. Biotechnol. Appl. Bioch. 18, 1–8.
Chicon, R., Belloque, J., Alonso, E. and Lopez-Fandino, R. (2009). Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure. Food Hydrocoll. 23, 593–599.
Cho, Y.J., Batt, C.A. and Sawyer, L. (1994a). Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 269, 11102–11107.
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, 263–270.
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, 252–255.
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 Hydrocoll. 6, 173–186.
Clement, G., Boquet, D., Frobert, Y., Bernard, H., Negroni, L., Chatel, J.M., Adel-Patient, K., Creminon, C., Wal, J.M. and Grassi, J. (2002). Epitopic characterization of native bovine β-lactoglobulin. J. Immunol. Methods 266, 67–78.
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.
Collini, M., D’Alfonso, L. and Baldini, G. (2000). New insight on β-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay. Protein Sci. 9, 1968–1974.
Collini, M., D’Alfonso, L., Molinari, H., Ragona, L., Catalano, M. and Baldini, G. (2003). Competitive binding of fatty acids and the fluorescent probe 1-8-anilinonaphthalene sulfonate to bovine β-lactoglobulin. Protein Sci. 12, 1596–1603.
Considine, T., Patel, H.A., Singh, H. and Creamer, L.K. (2005). Influence of binding of sodium dodecyl sulfate, all-trans-retinol, palmitate, and 8-anilino-1-naphthalenesulfonate on the heat-induced unfolding and aggregation of β-lactoglobulin B. J. Agric. Food Chem. 53, 3197–3205.
Considine, T., Patel, H.A., Anema, S.G., Singh, H. and Creamer, L.K. (2007). Interactions of milk proteins during heat and high hydrostatic pressure treatments—a review. Innov. Food Sci. Emerg. 8, 1–23.
Conti, A., Giuffrida, M.G., Napolitano, L., Quaranta, S., Bertino, E., Coscia, A., Costa, S. and Fabris, C. (2000). Identification of the human β-casein C-terminal fragments that specifically bind to purified antibodies to bovine β-lactoglobulin. J. Nutr. Biochem. 11, 332–337.
Cowan, S.W., Newcomer, M.E. and Jones, T.A. (1990). Crystallographic refinement of human serum retinol binding-protein at 2Å resolution. Proteins 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, 7170–7176.
Creamer, L.K., Bienvenue, A., Nilsson, H., Paulsson, M., van Wanroij, M., Lowe, E.K., Anema, S.G., Boland, M.J. and Jimenez-Flores, R. (2004). Heat-induced redistribution of disulfide bonds in milk proteins. 1. Bovine β-lactoglobulin. J. Agric. Food Chem. 52, 7660–7668.
Criscione, A., Cunsolo, V., Bordonaro, S., Guastella, A.M., Saletti, R., Zuccaro, A., D’Urso, G. and Marletta, D. (2009). Donkeys’ milk protein fraction investigated by electrophoretic methods and mass spectrometric analysis. Int. Dairy J. 19, 190–197.
Crittenden, R.G. and Bennett, L.E. (2005). Cow’s milk allergy: a complex disorder. J. Am. Coll. Nutr. 24, 582S–591S.
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, 137–143.
Cupo, J.F. and Pace, C.N. (1983). Conformational stability of mixed disulphide derivatives of β-lactoglobulin B. Biochemistry 22, 2654–2658.
D’Alfonso, L., Collini, M. and Baldini, G. (1999). Evidence of heterogeneous 1-anilinonaphthalene-8-sulfonate binding to β-lactoglobulin from fluorescence spectroscopy. Biochim. Biophys. Acta 1432, 194–202.
D’Alfonso, L., Collini, M. and Baldini, G. (2002). Does β-lactoglobulin denaturation occur via an intermediate state? Biochemistry 41, 326–333 and 2884.
D’Alfonso, L., Collini, M., Ragona, L., Ugolini, R., Baldini, G. and Molinari, H. (2005). Porcine β-lactoglobulin chemical unfolding: identification of a non-native α-helical intermediate. Proteins 58, 70–79.
Dar, T.A., Singh, L.R., Islam, A., Anjum, F., Moosavi-Movahedi, A.A. and Ahmad, F. (2007). Guanidinium chloride and urea denaturations of β-lactoglobulin A at pH 2.0.and 25 degrees C: the equilibrium intermediate contains non-native structures (helix, tryptophan and hydrophobic patches). Biophys. Chem. 127, 140–148.
Davidovic, M., Mattea, C., Qvist, J. and Halle, B. (2009). Protein cold denaturation as seen from the solvent. J. Am. Chem. Soc. 131, 1025–1036.
Davies, D.T. (1974). The quantitative partition of the albumin fraction of milk serum proteins by gel chromatography. J. Dairy Res. 41, 217–228.
Davis, B.D. and Dubos, R.J. (1947). The binding of fatty acids by serum albumin, a protective growth factor in bacteriological media. J. Exp. Med. 86, 215–228.
Davis, P.J. and Williams, S.C. (1998). Protein modification by thermal processing. Allergy 53, 102–105.
de Frutos, M., Cifuentes, A. and Díez-Masa, J.C. (1997) Multiple peaks in high-performance liquid chromatography of proteins - beta-lactoglobulins eluted in a hydrophobic interaction chromatography system. J. Chromatogr. A. 778, 43–52.
de Luis, R., Perez, M.D., Sanchez, L., Lavilla, M. and Calvo, M. (2007). Development of two immunoassay formats to detect β-lactoglobulin: influence of heat treatment on β-lactoglobulin immunoreactivity and assay applicability in processed food. J. Food Protect. 70, 1691–1697.
de Wit, J.N. (2009). Thermal behaviour of bovine β-lactoglobulin at temperatures up to 150º C. A review. Trends Food Sci .Tech. 20, 27–34.
de Wit, J.N. 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.
de Wolf, F.A. and Brett, G.M. (2000). Ligand-binding proteins: their potential for application in systems for controlled delivery and uptake of ligands. Pharmacol. Rev. 52, 207–236.
Denton, H., Husi, H., Smith, M.H., Uhrin, D., Barlow, P.N., Batt, C.A. and Sawyer, L. (1998). Preparation of double labelled protein for NMR studies from Pichia pastoris. Protein Expr. Purif. 14, 97–103.
Diaz de Villegas, M.C., Oria, R., Sala, F.J. and Calvo, M.(1987). Lipid binding by b-lactoglobulin of cow milk. Milchwissenschaft 42, 357–358.
Donald, A.M. (2008). Aggregation in β-lactoglobulin. Soft Matter 4, 1147–1150.
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. Biochemistry 35, 1450–1457.
Dorji, T., Namikawa, T., Mannen, H. and Kawamoto, Y. (2010). Milk protein polymorphisms in cattle (Bos indicus), mithun (Bos frontalis) and yak (Bos grunniens) breeds and their hybrids indigenous to Bhutan. Anim. Sci. J. 81, 523–529.
Dufour, E. and Haertlé, T. (1991). Binding of retinoids and β-carotene to β-lactoglobulin—influence of protein modifications. Biochim. Biophys. Acta 1079, 316–320.
Dufour, E. and Haertlé, T. (1993). Temperature-induced folding changes of β-lactoglobulin in hydro-methanolic solutions. Int. J. Biol. Macromol. 15, 293–297.
Dufour, E., Marden, M.C. and Haertlé, T. (1990). β-Lactoglobulin binds retinol and protoporphyrin-IX at 2 different binding-sites. FEBS Lett. 277, 223–226.
Dufour, E., Bertrand-Harb, C. and Haertlé, T. (1993). Reversible effects of medium dielectric-constant on structural transformation of β-lactoglobulin and its retinol binding. Biopolymers 33, 589–598.
Dufour, E., Genot, C. and Haertlé, T. (1994). β-Lactoglobulin binding-properties during its folding changes studied by fluorescence spectroscopy. Biochim. Biophys. Acta 1205, 105–112.
Dunnill, P. and Green, D.W. (1965). Sulphydryl groups and the N-R conformational change in β-lactoglobulin. J. Mol. Biol. 15, 147–151.
Eberini, I., Baptista, A.M., Gianazza, E., Fraternali, F. and Beringhelli, T. (2004). Reorganization in apo- and holo-β-lactoglobulin upon protonation of Glu89: molecular dynamics and pK α calculations Proteins 54, 744–758.
Eberini, I., Fantucci, P., Rocco, A.G., Gianazza, E., Galluccio, L., Maggioni, D., Dal Ben, I., Galliano, M., Mazzitello, R., Gaiji, N. and Beringhelli, T. (2006). Computational and experimental approaches for assessing the interactions between the model calycin β-lactoglobulin and two antibacterial fluoroquinolones. Proteins 65, 555–567.
Edelbauer, M., Loibichler, C., Nentwich, I., Gerstmayr, M., Urbanek, R. and Szepfalusi, Z. (2004). Maternally delivered nutritive allergens in cord blood and in placental tissue of term and preterm neonates. Clin. Exp. Allergy 34, 189–193.
Edwards, P.J.B., Jameson, G.B., Palmano, K.P. and Creamer, L.K. (2002). Heat-resistant structural features of bovine β-lactoglobulin A revealed by NMR H/D exchange observations. Int. Dairy J. 12, 331–344.
Edwards, P.B., Creamer, L.K. and Jameson, G.B. (2009). Structure and stability of whey proteins, in, Milk Proteins—From Expression to Food, A. Thompson, M. Boland and H. Singh, eds., Elsevier, Amsterdam. pp. 163–203.
Eichinger, A., Nasreen, A., Kim, H.J. and Skerra, A. (2007). Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D. J. Biol. Chem. 282, 31068–31075.
Eissa, A.S., Puhl, C., Kadla, J.F. and Khan, S.A. (2006). Enzymatic cross-linking of β-lactoglobulin: conformational properties using FTIR spectroscopy. Biomacromolecules 7, 1707–1713.
Elsik, C.G., Tellam, R.L., Worley, K.C., et al. and Zhu, B. (2009). The genome sequence of taurine cattle: a window to ruminant biology and evolution. Science 324, 522–528.
Evans, T.R.J. and Kaye, S.B. (1999). Retinoids: present role and future potential. Br. J. Cancer 80, 1–8.
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, 157–167.
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, 252–258.
Farrell, H.M. Jr., 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. and Swaisgood, H.E. (2004). Nomenclature of the proteins of cows’ milk—sixth revision. J. Dairy Sci. 87, 1641–1674.
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. Anim. Genet. 29, 473–474.
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, 43–46.
Ferry, J.D. and Oncley, J.L. (1941). Studies on the dielectric properties of protein solutions. III Lactoglobulin. J. Am. Chem. Soc. 63, 272–278.
Flower, D.R. (1996). The lipocalin protein family—structure and function. Biochem. J. 318, 1–14.
Fluckinger, M., Merschak, P., Hermann, M., Haertlé, T. and Redl, B. (2008). Lipocalin-interacting-membrane-receptor (LIMR) mediates cellular internalization of β-lactoglobulin. Biochim. Biophys. Acta—Biomembranes 1778, 342–347.
Foegeding, E.A. (2006). Food biophysics of protein gels: a challenge of nano and macroscopic proportions. Food Biophys. 1, 41–50.
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, 149–154.
Fogolari, F., Ragona, L., Licciardi, S., Romagnoli, S., Michelutti, R., Ugolini, R. and Molinari, H. (2000). Electrostatic properties of bovine β-lactoglobulin. Proteins 39, 317–330.
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 native-like β-sheet and non-native α-helix. J. Mol. Biol. 296, 1039–1051.
Fox, P.F. (1995). Heat induced changes in milk, 2nd edn. IDF Special Issue No. 9501. International Dairy Federation, Brussels.
Frapin, D., Dufour, E. and Haertlé, T. (1993). Probing the fatty-acid-binding site of β-lactoglobulins. J. Protein Chem. 12, 443–449.
Fraser, R.M., Keszenman-Pereyra, D., Simmen, M.W. and Allan, J. (2009). High-resolution mapping of sequence-directed nucleosome positioning on genomic DNA. J. Mol. Biol. 390, 292–305.
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, 4455–4463.
Fujiwara, K., Ikeguchi, M. and Sugai, S. (2001). A partially unfolded state of equine β-lactoglobulin at pH 8.7. J. Protein Chem. 20, 131–137.
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. Am. J. Clin. Nutr. 65, 30–35.
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, 5168–5172.
Ganai, N.A., Bovenhuis, H., van Arendonk, J.A.M. and Visker, M.H.P.W. (2009). Novel polymorphisms in the bovine β-lactoglobulin gene and their effects on β-lactoglobulin protein concentration in milk. Anim. Genet. 40, 127–133.
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. U S A 88, 2456–2460.
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, 1097–1107.
Georges, C. and Guinand, S. (1960). Sur la dissociation reversible de la β-lactoglobuline, à des pH superieurs à 5.5. 1. Étude par la diffusion de la lumiere. J. Chim. Phys. 57, 606–614.
Georges, C., Guinand, S. and Tonnelat, J. (1962). Étude thermodynamique de la dissociation reversible de la β-lactoglobuline B pour des pH superieurs à 5.5. Biochim. Biophys. Acta 59, 737–739.
German, T. and Barash, I. (2002). Characterization of an epithelial cell line from bovine mammary gland. In Vitro Cell. Dev. Biol. Anim. 38, 282–292.
Gestin, M., Desbois, C., Le Huërou-Luron, I., Romé, V., Le Dréan, 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-induced interactions and gelation of mixtures of β-lactoglobulin and α-lactalbumin. J. Agric. Food Chem. 45, 1130–1136.
Ghose, A.C., Chaudhuri, S. and Sen, A. (1968). Hydrogen ion equilibria and sedimentation behaviour of goat β-lactoglobulins. Arch. Biochem. Biophys. 126, 232–243.
Godovac-Zimmermann, J., Conti, A., Liberatori, J. and Braunitzer, G. (1985). 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, 601–608.
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, 1313–1319.
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, 171–179.
Godovac-Zimmermann, J., Krause, I., Buchberger, J., Weiss, G. and Klostermeyer, H. (1990). Genetic-variants of bovine β-lactoglobulin—a novel wild-type β-lactoglobulin W and its primary sequence. Biol. Chem. Hoppe-Seyler 371, 255–260.
Godovac-Zimmermann, J., Krause, I., Baranyi, M., Fischer-Fruhholz, 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. Protein Chem. 15, 743–750.
Gordon, E.J., Leonard, G.A., McSweeney, S. and Zagalsky, P.F. (2001). The C-1 subunit of α-crustacyanin: the de novo phasing of the crystal structure of a 40 kDa homodimeric protein using the anomalous scattering from S atoms combined with direct methods. Acta Crystallogr. D57, 1230-1237.
Gottschalk, M., Nilsson, H., Roos, H. and Halle, B. (2003). Protein self-association in solution: the bovine β-lactoglobulin dimer and octamer. Protein Sci. 12, 2404-2411.
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., North, A.C.T. and Aschaffenburg, R. (1956). Crystallography of β-lactoglobulin from cow’s milk. Biochim. Biophys. Acta 21, 583-585.
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, 375-397.
Grönwall, A. (1942). Studies on the solubility of lactoglobulin. C.R. Trav. Lab. Carls. Ser. Chim. 24, 185-200.
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, 461-479.
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. Am. Chem. Soc. 73, 2790-2793.
Grzyb, J., Latowski, D. and Strzalka, K. (2006). Lipocalins—a family portrait. J. Plant Physiol. 163, 895-915.
Guichard, E. (2006). Flavour retention and release from protein solutions. Biotechnol. Adv. 24, 226-229.
Gulzar, M., Croguennec, T., Jardin, J., Piot, M. and Bouhallab, S. (2009). Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of β-lactoglobulin. Food Chem. 116, 884-891.
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, 2336-2344.
Guo, H.Y., Pang, K., Zhang, X.Y., Zhao, L., Chen, S.W., Dong, M.L. and Ren, F.Z. (2007). Composition, physiochemical properties, nitrogen fraction distribution, and amino acid profile of donkey milk. J. Dairy Sci. 90, 1635-1643.
Guth, H. and Fritzler, R. (2004). Binding studies and computer-aided modelling of macromolecule/ odorant interactions. Chem. Biodivers. 1, 2001-2023
Hajoubi, S., Rival-Gervier, S., Hayes, H., Floriot, S., Eggen, A., Piumi, F., Chardon, P., Houdebine, L.M. and Thepot, D. (2006). Ruminants genome no longer contains whey acidic protein gene but only a pseudogene. Gene 370, 104-112.
Hall, A.J., Masel, A., Bell, K., Halliday, J.A., Shaw, D.C. and VandeBerg, J.L. (2001). Characterization of baboon (Papio hamadryas) milk proteins. Biochem. Genet. 39, 59-71.
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, 8629-8633.
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.
Hamada, D. and Goto, Y. (1997). The equilibrium intermediate of β-lactoglobulin with non-native α-helical structure. J. Mol. Biol. 269, 479-487.
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, 737-746.
Hamada, D., Segawa, S. and Goto, Y. (1996). Non-native α-helical intermediate in the refolding of β-lactoglobulin, a predominantly β-sheet protein. Nat. Struct. Biol. 3, 868-873.
Hamada, D., Tanaka, T., Tartaglia, G.G., Pawar, A., Vendruscolo, M., Kawamura, M., Tamura, A., Tanaka, N. and Dobson, C.M. (2009). Competition between folding, native-state dimerisation and amyloid aggregation in β-lactoglobulin. J. Mol. Biol. 386, 878-890.
Hambling, S.G., McAlpine, A.S. and Sawyer, L. (1992). β-lactoglobulin, in, Advanced Dairy Chemistry I, P.F. Fox, ed., Elsevier, Amsterdam. pp. 140-191.
Harvey, B.J., Bell, E. and Brancaleon, L. (2007). A tryptophan rotamer located in a polar environment probes pH-dependent conformational changes in bovine β-lactoglobulin A. J. Phys. Chem. B 111, 2610-2620.
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, 22414-22419.
Hattori, M., Miyakawa, S., Ohama, Y., Kawamura, H., Yoshida, T., To-O, K., Kuriki, T. and Takahashi, K. (2004). Reduced immunogenicity of β-lactoglobulin by conjugation with acidic oligosaccharides. J. Agric. Food Chem. 52, 4546-4553.
Hazebrouck, S., Pothelune, L., Azevedo, V., Corthier, G., Wal, J.-M. and Langella, P. (2007). Efficient production and secretion of bovine β-lactoglobulin by Lactobacillus casei. Microb. Cell Fact. 6, Article Number: 12.
Heddleson, R.A., Allen, 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, 2369-2373.
Heikura, J., Suutari, T., Rytkonen, J., Nieminen, M., Virtanen, V. and Valkonen, K. (2005). A new procedure to isolate native β-lactoglobulin from reindeer milk. Milchwissenschaft 60, 388-392.
Hemley, R., Kohler, B.E. and Siviski, P. (1979). Absorption spectra for the complexes formed from vitamin-A and β-lactoglobulin. Biophys. J. 28, 447-455.
Hemung, B.-O., Li-Chan, E.C.Y. and Yongsawatdigul, J. (2009). Identification of glutaminyl sites on β-lactoglobulin for threadfin bream liver and microbial transglutaminase activity by MALDI-TOF mass spectrometry. Food Chem. 115, 149-154.
Hennighausen, L.G. and Sippel, A.E. (1982). Mouse whey acidic protein is a novel member of the family of ‘four-disulphide core’ proteins. Nucleic Acids Res. 10, 2677-2684.
Hernandez-Ledesma, B., Recio, I. and Amigo, L. (2008). β-Lactoglobulin as source of bioactive peptides. Amino Acids 35, 257-265.
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. Am. Chem. Soc. 86, 4445-4452.
Hill, A.R. (1989). The β-lactoglobulin-κ-casein complex. Can. Inst. Food Sci. Tech. J. 22, 120-123.
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. ACS Symposium Series 650, 281-294.
Hirano, A., Maeda, Y., Akasaka, T. and Shiraki, K. (2009). Synergistically enhanced dispersion of native protein-carbon nanotube conjugates by fluoroalcohols in aqueous solution. Chem. Eur. J. 15, 9905-9910.
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.
Hoedemaeker, F.J., Visschers, R.W., Alting, A.C., de Kruif, K.G., Kuil, M.E. and Abrahams, J.P. (2002). A novel pH-dependent dimerization motif in β-lactoglobulin from pig (Sus scrofa). Acta Crystallogr. D 58, 480-486.
Holmes, M.A., Paulsene, W., Jide, X., Ratledge, C. and Strong, R.K. (2005). Siderocalin (LCN 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure 13, 29-41.
Holt, C., Waninge, R., Sellers, P., Paulsson, M., Bauer, R., Ogendal, L., Roefs, S.P.F.M., vanMill, 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.
Holt, C., McPhail, D., Nylander, T., Otte, J., Ipsen, R.H., Bauer, R., Ogendal, L., Olieman, K., de Kruif, K.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.
Hubbard, T.J.P., Aken, B.L., Ayling, S., et al. Flicek, P. (2009). Ensembl 2009. Nucleic Acids Res. 37, D690-D697.
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.
Hudson, G.J., Bailey, P.A., John, P.M.V., Monsalve, L., Delcampo, A.L.G., Taylor, D.C. and Kay, J.D.S. (1984). Composition of milk from Ailuropoda melanoleuca, the giant panda. Vet. Record 115, 252-252.
Hui Bon Hoa, G., Guinand, S., Douzou, P. and Pantaloni, C. (1973). Transformations alcalines de la β-lactoglobulies en milieau hydro-alcoolique à basses temperatures. Biochimie 55, 269-276.
Hunziker, H.G. and Tarassuk, N.P. (1965). Chromatographic evidence for heat induced interaction of α-lactalbumin and β-lactoglobulin. J. Dairy Sci. 48, 733-744.
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, 191-198.
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, 23-29.
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, 2159-2166.
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 27, 567-575.
Imre, T., Zsila, F. and Szabo, P.T. (2003). Electrospray mass spectrometric investigation of the binding of cis-parinaric acid to bovine β-lactoglobulin and study of the ligand-binding site of the protein using limited proteolysis. Rapid Comm. Mass Spect. 17, 2464-2470.
Invernizzi, G., Ragona, L., Brocca, S., Pedrazzoli, E., Molinari, H., Morandini, P., Catalano, M. and Lotti, M. (2004). Heterologous expression of bovine and porcine β-lactoglobulins in Pichia pastoris: towards a comparative functional characterization. J. Biotechnol. 109, 169-178.
Invernizzi, G., Samalikova, M., Brocca, S., Lotti, M., Molinari, H. and Grandori, R. (2006). Comparison of bovine and porcine β-lactoglobulin: a mass spectrometric analysis. J. Mass Spect. 41, 717-727.
Invernizzi, G., Annoni, E., Natalello, A., Doglia, S.M. and Lotti, M. (2008). In vivo aggregation of bovine β-lactoglobulin is affected by Cys at position 121. Protein Expr. Purif. 62, 111-115.
Ivanov, V.N., Judinkova, E.S. and Gorodetsky, S.I. (1988). Molecular cloning of bovine β-lactoglobulin cDNA. Biol. Chem. Hoppe-Seyler 369, 425-429.
Izquierdo, F. J., Alli, I., Yaylayan, V. and Gomez, R. (2007). Microwave-assisted digestion of β-lactoglobulin by pronase, α-chymotrypsin and pepsin. Int. Dairy J. 17, 465-470.
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. Anim. Genet. 23, 77–79.
Jakob, E. and Puhan, Z. (1992). Technological properties of milk as influenced by genetic polymorphism of milk proteins—a review. Int. Dairy J. 2, 157–178.
Jameson, G.B., Adams, J.J., Creamer, L.K. (2002). Flexibility, functionality and hydrophobicity of bovine β-lactoglobulin. Int. Dairy J. 12, 319–329.
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, 2067–2074.
Jarvinen, K.M., Chatchatee, P., Bardina, L., Beyer, K. and Sampson, H.A. (2001). IgE and IgG binding epitopes on α-lactalbumin and β-lactoglobulin in cow’s milk allergy. Int. Arch. Allergy Immunol. 126, 111–118.
Jayat, D., Gaudin, J.-C., Chobert, J.-M., Burova, T.V., Holt, C., McNae, I., Sawyer, L. and Haertlé, T. (2004). A C121S mutation of bovine β-lactoglobulin leads to decreased stability of the protein to peptic digestion, reducing agents and heating. Biochemistry 43, 6312–6321.
Jenness, R. (1979). Comparative aspects of milk proteins. J. Dairy Res. 46, 197–210.
Jenness, R. (1985). Biochemical and nutritional aspects of milk and colostrums, in, Lactation, B.L. Larson, ed., The Iowa State University Press, Ames. pp. 164–197.
Jenness, R., Erickson, A.W. and Craighead, J.J. (1972). Some comparative aspects of milk from 4 species of bears. J. Mammal. 53, 34–47.
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, 80–85.
Jiang, H.R. and Liu, N. (2010). Self-assembled β-lactoglobulin-conjugated linoleic acid complex for colon cancer-targeted substance. J. Dairy Sci. 93, 3931–3939.
Jones, S.B. and Kalan, E.B. (1971). Modified procedure for isolation of a major swine whey protein. J. Dairy Sci. 54, 288–291.
Joss, J.L., Molloy, M.P., Hinds, L. and Deane, E. (2009). A longitudinal study of the protein components of marsupial milk from birth to weaning in the tammar wallaby (Macropus eugenii). Dev. Comp. Immunol. 33, 152–161.
Jouenne, E. and Crouzet, J. (2000). Determination of apparent binding constants for aroma compounds with β-lactoglobulin by dynamic coupled column liquid chromatography. J. Agric. Food Chem. 48, 5396–5400.
Jun, S. and Puri, V.M. (2005). Fouling models for heat exchangers in dairy processing: a review. J. Food Process Eng. 28, 1–34.
Kaddouri, H., Mimoun, S., El-Mecherfi, K.E., Chekroun, A., Kheroua, O. and Saidi, D. (2008). Impact of γ-radiation on antigenic properties of cow’s milk β-lactoglobulin. J. Food Protect. 71, 1270–1272.
Kalan, E.B. and Basch, J.J. (1969). Preparation of goat β-lactoglobulin. J. Dairy Sci. 49, 406–409.
Kalidas, C., Joshi, L. and Batt, C.A. (2001). Characterization of glycosylated variants of β-lactoglobulin expressed in Pichia pastoris. Protein Eng. 14, 201–207.
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, 50–56.
Kappeler, S.R., Farah, Z. and Puhan, Z. (2003). 5¢-Flanking regions of camel milk genes are highly similar to homologue regions of other species and can be divided into two distinct groups. J. Dairy Sci. 86, 498–508.
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, 133–141.
Katou, H., Hoshino, M., Kamikubo, H., Batt, C.A. and Goto, Y. (2001). Native-like β-hairpin retained in the cold-denatured state of bovine β-lactoglobulin. J. Mol. Biol. 310, 471–484.
Kessler, E. and Brew, K. (1970). The whey proteins of pig’s milk isolation and characterization of a β-lactoglobulin. Biochim. Biophys. Acta 200, 449–458.
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, 1339–1345.
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 probed by hydrogen exchange. J. Mol. Biol. 299, 757–770.
Kobayashi, T., Ikeguchi, M. and Sugai, S. (2002). Construction and characterization of β-lactoglobulin chimeras. Proteins 49, 297–301.
Kolde, H.J., Liberatori, J. and Braunitzer, G. (1981). The amino-acid-sequence of the water buffalo β-lactoglobulin. Milchwissenschaft 36, 83–86.
Kontopidis, G., Holt, C. and Sawyer, L. (2002). Retinol binding to bovine β-lactoglobulin. J. Mol. Biol. 318, 1043–1055.
Kontopidis, G., Holt, C. and Sawyer, L. (2004). Invited Review: β-Lactoglobulin: binding properties, structure, and function. J. Dairy Sci. 87, 785–796.
Konuma, T., Sakurai, K. and Goto, Y. (2007). Promiscuous binding of ligands by β-lactoglobulin involves hydrophobic interactions and plasticity. J. Mol. Biol. 368, 209–218.
Kotresh, A.M., Arunkumar, G.B., Kanthraj, C., Saxena, M. and Sharma, B. (2009). Structural features of the 5¢-flanking region of the β-lactoglobulin gene of buffalo (Bubalus bubalis). Buffalo Bull. 28, 34–39.
Krebs, M.R.H., Devlin, G.L. and Donald, A.M. (2007). Protein particulates: another generic form of protein aggregation? Biophys. J. 92, 1336–1342.
Krebs, M.R.H., Domike, K.R. and Donald, A.M. (2009). Protein aggregation: more than just fibrils. Biochem. Soc. Trans. 37, 682–686.
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, 113–118.
Kühn, J., Considine, T. and Singh, H. (2006). Interactions of milk proteins and volatile flavor compounds: implications in the development of protein foods. J. Food Sci. 71, R72–R82.
Kumasaka, T., Aritake, K., Ago, H., Irikura, D., Tsurumura, T., Yamamoto, M., Miyano, M., Urade, Y. and Hayaishi, O. (2009). Structural basis of the catalytic mechanism operating in open-closed conformers of lipocalin type prostaglandin D synthase. J. Biol. Chem. 284, 22344–22352.
Kunz, C. and Lönnerdal, B. (1994). Isolation and characterization of a 21 kDa whey-protein in rhesus-monkey (Macaca mulatta) milk. Comp. Biochem. Physiol. B 108, 463–469.
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, 2069–2075.
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, 1733–1737.
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, 115–118.
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, 731–739.
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, 2541–2545.
Kuwata, K., Shastry, R., Cheng, H., Hoshino, M., Batt, C.A., Goto, Y. and Roder, H. (2001). Structural and kinetic characterization of early folding events in β-lactoglobulin. Nat. Struct. Biol. 8, 151–155.
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, 2896–2903.
Lamiot, E., Dufour, E. and Haertlé, T. (1994). Insect sex-pheromone binding by bovine β-lactoglobulin. J. Agric. Food Chem. 42, 695–699.
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.
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, 506–510.
Lemay, D.G., Lynn, D.J., Martin, W.F., et al. and Rijnkels, M. (2009). The bovine lactation genome: insights into the evolution of mammalian milk. Genome Biol. 10(4), Article R43.
Leonil, J., Molle, D., Gaucheron, F., Arpino, P., Guenot, P. and Maubois, J.L. (1995). Analysis of major bovine-milk proteins by online high-performance liquid-chromatography and electrospray-ionization mass-spectrometry. Lait 75, 193–210.
Li, C.H. (1946). Electrophoretic inhomogeneity of crystalline β-lactoglobulin. J. Am. Chem. Soc. 68, 2746–2747.
Li, H., Hardin, C.C. and Foegeding, E.A. (1994). NMR-studies of thermal-denaturation and cation-mediated aggregation of β-lactoglobulin. J. Agric. Food Chem. 42, 2411–2420.
Liberatori, J., Guidetti, M.L. and Conti, A. (1979a). 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, 815–821.
Liberatori, J., Guidetti, M.L. and Conti, A. (1979b). Immunological evidence of β-lactoglobulins. In human colostrums and milk. Boll. Soc. It. Biol. Sper. 55, 822–825.
Liberatori, J., Guidetti, M.L., Conti, A. and Napolitano, L. (1979c). 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, 1369–1373.
Lien, S., Alestrom, P., Steine, T., Langsrud, T., Vegarud, G. and Rogne, S. (1990). A method for β-lactoglobulin genotyping of cattle. Livest. Prod. Sci. 25, 173–176.
Loch, J., Polit, A., Gorecki, A., Bonarek, P., Kurpiewska, K., Dziedzicka-Wasylewska, M. and Lewinski, K. (2011). Two modes of fatty acid binding to bovine β-lactoglobulin-crystallographic and spectroscopic studies. J. Mol. Recog. 24, 341–349.
Loch, J.I., Polit, A., Bonarek, P., Olszewska, D., Kurpiewska, K., Dziedzicka-Wasylewska, M. and Lewinski, K. (2012). Structural and thermodynamic studies of binding saturated fatty acids to bovine beta-lactoglobulin. Int. J. Biol. Macromol. 50, 1095–1102.
Loveday, S.M. and Singh, H. (2008). Recent advances in technologies for vitamin A protection in foods. Trends Food Sci. Tech. 19, 657–668.
Lovrien, R. and Anderson, W.F. (1969). Resolution of binding sites in β-lactoglobulin. Arch. Biochem. Biophys. 131, 139–144.
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, 663–666.
Lowe, E.K., Anema, S.G., Bienvenue, A., Boland, M.J., Creamer, L.K. and Jimenez-Flores, R. (2004). Heat-induced redistribution of disulfide bonds in milk proteins. 2. Disulfide bonding patterns between bovine β-lactoglobulin and kappa-casein. J. Agric. Food Chem. 52, 7669–7680.
Lozano, J.M., Giraldo, G.I. and Romero, C.M. (2008). An improved method for isolation of β-lactoglobulin. Int. Dairy J. 18, 55–63.
Lu, R.C., Cao, A.N., Lai, L.H. and Xiao, J.X. (2006). Interactions of β-lactoglobulin with sodium decylsulfonate, decyltriethylammonium bromide, and their mixtures. J. Colloid Interf. Sci. 299, 617–625.
Lübke, M., Guichard, E., Tromelin, A. and Le Quere, J.L. (2002). Nuclear magnetic resonance spectroscopic study of β-lactoglobulin interactions with two flavor compounds, γ-decalactone and β-ionone J. Agric. Food Chem. 50, 7094–7099.
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., Jenness, R., Phillips, N.I. and Sloan, R.E. (1966). Comparative biochemical studies of milks. 3. Immunoelectrophoretic comparisons of milk proteins of Artiodactyla. Comp. Biochem. Physiol. 17, 967–971.
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.
Magdassi, S., Vinetsky, Y. and Relkin, P. (1996). Formation and structural heat-stability of β-lactoglobulin/surfactant complexes. Colloid Surf. B 6, 353–362.
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, 743–745.
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, 5052–5061.
Manderson, G.A., Creamer, L.K. and Hardman, M.J. (1999a). Effect of heat treatment on the circular dichroism spectra of bovine β-lactoglobulin A, B and C. J. Agric. Food Chem. 47, 4557–4567.
Manderson, G.A., Hardman, M.J. and Creamer, L.K. (1999b). Effect of heat treatment on bovine β-lactoglobulin A, B and C explored using thiol availability and fluorescence. J. Agric. Food Chem. 47, 3617–3627.
Mansouri, A., Haertle, T., Gerard, A., Gerard, H. and Gueant, J.L. (1997). Retinol free and retinol complexed β-lactoglobulin binding sites in bovine germ cells. Biochim. Biophys. Acta—Mol. Cell Res. 1357, 107–114.
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, 258–262.
Martins, P.A.T., Gomes, F., Vaz, W.L.C. and Moreno, M. J. (2008). Binding of phospholipids to β-lactoglobulin and their transfer to lipid bilayers. Biochim. Biophys. Acta—Biomembranes 1778, 1308–1315.
Matsumura, Y., Li, J., Ikeguchi, M. and Kihara, H. (2008). Helix-rich transient and equilibrium intermediates of equine β-lactoglobulin in alkaline buffer. Biophys. Chem. 134, 84–92.
Maubois, J.L., Pion, R. and Ribadeau-Dumas, B. (1965). Preparation et etude de la β-lactoglobulin de brebis crystallisée B. Biochim. Biophys. Acta 107, 501–510.
McAlpine, 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, 259–264.
McDougall, E.I. and Stewart, J.C. (1976). Whey proteins of milk of red deer (Cervus elaphus L)—homologue of bovine β-lactoglobulin. Biochem. J. 153, 647–655.
McKenzie, H.A. (1967). Milk proteins. Adv. Protein Chem. 22, 56–234.
McKenzie, H.A. (1971). β-lactoglobulins, in, Milk Proteins: Chemistry and Molecular Biology, Vol. 2, H.A. McKenzie, ed., Academic, New York. pp. 257–330.
McKenzie, H.A. and Sawyer, W.H. (1967). Effect of pH on β-lactoglobulins. Nature 214, 1101–1104.
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 New Biol. 238, 147–149.
McKenzie, H.A., Ralston, G.B. and Shaw, D.C. (1972). Location of sulphydryl and disulphide groups in bovine ß-lactoglobulins and effects of urea. Biochemistry 11, 4539–4547.
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. B 74, 259–271.
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, 451–457.
Mercadé-Prieto, R., Wilson, D.I. and Paterson, W.R. (2008). Effect of the NaOH concentration and temperature on the dissolution mechanisms of β-lactoglobulin gels in alkali. Int. J. Food Eng. 4(5), Article 9.
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-, κ-casein and β-lactoglobulin. Nucleotide sequence of αs1-casein cDNA. Biochimie 67, 959–971.
Mierzejewska, D. and Kubicka, E. (2006). Effect of temperature on immunoreactive properties of the cow milk whey protein β-lactoglobulin. Milchwissenschaft 61, 69–72.
Mills, O.E. and Creamer, L.K. (1975). Conformational changes of bovine β-lactoglobulin at low pH. Biochim. Biophys. Acta 379, 618–626.
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.
Miranda, G., Mahe, M.F., Leroux, C. and Martin, P. (2004). Proteomic tools to characterize the protein fraction of Equidae milk. Proteomics 4, 2496–2509.
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, 246–255.
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, 237–243.
Monaci, L., Tregoat, V., van Hengel, A.J. and Anklam, E. (2006). Milk allergens, their characteristics and their detection in food: a review. Eur. Food Res. Technol. 223, 149–179.
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.
Moreno, F.J. (2007). Gastrointestinal digestion of food allergens: effect on their allergenicity. Biomed. Pharmacother. 61, 50–60.
Nakagawa, K., Tokushima, A., Fujiwara, K. and Ikeguchi, M. (2006). Proline scanning mutagenesis reveals non-native fold in the molten globule state of equine β-lactoglobulin. Biochemistry 45, 15468–15473.
Nakagawa, K., Yamada, Y., Fujiwara, K. and Ikeguchi, M. (2007). Interactions responsible for secondary structure formation during folding of equine β-lactoglobulin. J. Mol. Biol. 367, 1205–1214.
Narayan, M. and Berliner, L.J. (1997). Fatty acids and retinoids bind independently and simultaneously to β-lactoglobulin. Biochemistry 36, 1906–1911.
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, 150–157.
Nath, N.C., Hussain, A. and Rahman, F. (1993). Milk characteristics of a captive Indian rhinoceros (Rhinoceros unicornis). J. Zoo Wildlife Med. 24, 528–533.
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. Nat. Med. 2, 230–234.
Niemi, M., Jylha, S., Laukkanen, M.L., Soderlund, H., Makinen-Kiljunen, S., Kallio, J.M., Hakulinen, N., Haahtela, T., Takkinen, K. and Rouvinen, J. (2007). Molecular interactions between a recombinant IgE antibody and the β-lactoglobulin allergen. Structure 15, 1413–1421.
Nieuwenhuizen, W.F., Dekker, H.L., Groneveld, T., de Koster, C.G. and de Jong, G.A.H. (2004). Transglutaminase-mediated modification of glutamine and lysine residues in native bovine β-lactoglobulin. Biotech. Bioeng. 85, 248–258.
North, A.C.T. (1989). Three-dimensional arrangement of conserved amino acids in a superfamily of specific ligand-binding proteins. Int. J. Biol. Macromol. 11, 56–58.
North, A.C.T. (1991). Structural homology in ligand specific transport proteins. Biochem. Soc. Symp. 57, 35–48.
O’Neill, T. and Kinsella, J.E. (1988). Effect of heat-treatment and modification on conformation and flavor binding by β-lactoglobulin. J. Food Sci. 53, 906–909.
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, 105–124.
Ohtomo, H., Konuma, T., Utsunomiya, H., Tsuge, H. and Ikeguchi, M. (2011). Structure and stability of Gyuba, a β-lactoglobulin chimera. Protein Sci. 20, 1867–1875.
Oksanen, E., Jaakola, V.P., Tolonen, T., Valkonen, K., Akerstrom, B., Kalkkinen, N., Virtanen, V. and Goldman, A. (2006). Reindeer β-lactoglobulin crystal structure with pseudo-body-centred noncrystallographic symmetry. Acta Crystallogr. D 62, 1369–1374.
Oliveira, K.M.G., Valente-Mesquita, V.L., Botelho, M.M., Sawyer, L., Ferreira, S.T. and Polikarpov, I. (2001). Crystal structures of bovine β-lactoglobulin in the orthorhombic space group C222(1)—structural differences between genetic variants A and B and features of the Tanford transition. Eur. J. Biochem. 268, 477–483.
Oliveira, C.L.P., de la Hoz, L., Silva, J.C., Torriani, I.L. and Netto, F.M. (2006). Effects of γ radiation on β-lactoglobulin: oligomerization and aggregation. Biopolymers 85, 284–294; and correction: 87, 93–93.
O’Neill, T.E. and Kinsella, J.E. (1987). Binding of alkanone flavors to β-lactoglobulin: effects of conformational and chemical modification. J. Agric. Food Chem. 35, 770–774.
Ortlund, E., Parker, C.L., Schreck, S.F., Ginell, S., Minor, W., Sodetz, J.M. and Lebioda, L. (2002). Crystal structure of human complement protein C8γ at 1.2 Å resolution reveals a lipocalin fold and a distinct ligand binding site. Biochemistry 41, 7030–7037.
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, 685–692.
Pace, N.C. and Tanford, C. (1968). Thermodynamics of the unfolding of β-lactoglobulin A in aqueous urea solutions between 5 and 55. Biochemistry 7, 198-208.
Palmer, A.H. (1934). The preparation of a crystalline globulin from the albumin fraction of cow’s milk. J. Biol. Chem. 104, 359–372.
Palupi, N.S., Franck, P., Guimont, C., Linden, G., Dumas, D., Stoltz, J., Nabet, P., Belleville-Nabet, F. and Dousset, B. (2000). Bovine β-lactoglobulin receptors on transformed mammalian cells (hybridomas MARK-3): characterization by flow cytometry. J. Biotechnol. 78, 171–184.
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. Biochemistry 38, 6512–6519.
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, 383–385.
Passey, R.J. and Mackinlay, A.G. (1995). Characterization of a 2nd, apparently inactive, copy of the bovine β-lactoglobuln gene. Eur. J. Biochem. 233, 736–743.
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, 2637–2644.
Pellegrini, A. (2003). Antimicrobial peptides from food proteins. Curr. Pharm. Design 9, 1225–1238.
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, 1506–1509.
Pena, R.N. and Whitelaw, C.B.A. (2005). Duplication of Stat5-binding sites within the β-lactoglobulin promoter compromises transcription in vivo. Biochimie 87, 523–528.
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. Mamm. Genome 10, 560–564.
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, 978–988.
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, 1094–1097.
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, 151–155.
Pérez, M.D., Puyol, P., Ena, J.M. and Calvo, M. (1993). Comparison of the ability to bind lipids of β-lactoglobulin and serum-albumin of milk from ruminant and non-ruminant species. J. Dairy Res. 60, 55–63.
Perez-Miller, S., Zou, Q., Novotny, M.V. and Hurley, T.D. (2010). High resolution X-ray structures of mouse major urinary protein nasal isoform in complex with pheromones. Protein Sci. 19, 1469–1479.
Pervaiz, S. and Brew, K. (1985). Homology of β-lactoglobulin, serum retinol-binding protein and protein HC. Science 228, 335–337.
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, 846–854.
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, 209–214.
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 self-associating 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, 511–516.
Phillips, N.I., Jenness, R. and Kalan, E.B. (1968). Immunochemical comparison of β-lactoglobulins. J. Immunol. 100, 307–313.
Piazza, R., Iacopini, S. and Galliano, M. (2002). BLGA protein solutions at high ionic strength: vanishing attractive interactions and “frustrated” aggregation. Europhys. Lett. 59, 149–154.
Piez, K.A., Davie, E.W., Folk, J.E. and Gladner, J.A. (1961). β-Lactoglobulins A and B. J. Biol. Chem. 236, 2912–2916.
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, Marsupialia). J. Mol. Evol. 46, 361–369.
Polis, P.D., Schmuckler, H.W., Custer, J.H. and McMeekin, T.L. (1950). Isolation of an electrophoretically homogenous crystalline component of β-lactoglobulin. J. Am. Chem. Soc. 72, 4965–4968.
Ponniah, K., Loo, T.S., Edwards, P.J.B., Pascal, S.M., Jameson, G.B. and Norris, G.E. (2010). The production of soluble and correctly folded recombinant bovine β-lactoglobulin variants A and B in Escherichia coli for NMR studies. Protein Expr. Purif. 70, 283–289.
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, 980–981.
Préaux, G., Braunitzer, G., Schrank, B. and Stangl, A. (1979). The amino acid sequence of goat β-lactoglobulin. Hoppe Seyler’s Z. Physiol. Chem. 360, 1595–1604.
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, 325–333.
Prinzenberg, E.M. and Erhardt, G. (1999). Molecular genetic characterization of ovine β-lactoglobulin C allele and detection by PCR-rflp. J. Anim. Breed. Genet. 116, 9–14.
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, 193–199.
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, 2515–2520.
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, 149–154.
PyMOL. (2008). The PyMOL Molecular Graphics System, Version 1.1r1, Schrödinger, LLC.
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, 43–49.
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, 341–346.
Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, H.M., Baker, E.N. and Jameson, G.B. (1998a). Structural basis of the Tanford transition of bovine β-lactoglobulin. Biochemistry 37, 14014–14023.
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, 272–278.
Qin, B.Y., Bewley, M.C., Creamer, L.K., Baker, E.N. and Jameson, G.B. (1999). Functional implications of structural differences between variants A and B of bovine β-lactoglobulin. Protein Sci. 8, 75–83.
Qvist, J., Davidovic, M., Hamelberg, D. and Halle, B. (2008). A dry ligand-binding cavity in a solvated protein. Proc. Natl. Acad. Sci. U S A 105, 6296–6301.
Rachagani, S., Gupta, I.D., Gupta, N. and Gupta, S.C. (2006). Genotyping of β-lactoglobulin gene by PCR-RFLP in Sahiwal and Tharparkar cattle breeds. BMC Genetics 7, 31.
Ragona, L., Pusterla, 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. Fold. Des. 2, 281–290.
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, 953–969.
Ragona, L., Fogolari, F., Zetta, L., Perez, D.M., Puyol, P., De Kruif, K., Lohr, F., Ruterjans, H. and Molinari, H. (2000). Bovine β-lactoglobulin: interaction studies with palmitic acid. Protein Sci. 9, 1347–1356.
Ragona, L., Fogolari, F., Catalano, M., Ugolini, R., Zetta, L. and Molinari, H. (2003). EF loop conformational change triggers ligand binding in β-lactoglobulins. J. Biol. Chem. 278, 38840–38846.
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, London. pp. 235–252.
Reichenstein, M., German, T. and Barash, I. (2005). BLG-e1—a novel regulatory element in the distal region of the β-lactoglobulin gene promoter. FEBS Lett. 579, 2097–2104.
Reiners, J., Nicklaus, S. and Guichard, E. (2000). Interactions between β-lactoglobulin and flavour compounds of different chemical classes. Impact of the protein on the odour perception of vanillin and eugenol. Lait 80, 347–360.
Relkin, P. (1996). Thermal unfolding of β-lactoglobulin, α-lactalbumin and bovine serum-albumin—a thermodynamic approach. Crit. Rev. Food Sci. Nutr. 36, 565–601.
Relkin, P. and Vermersh, J. (2001). Binding properties of vanillin to whey proteins: effect on protein conformational stability and foaming properties, in, Food Colloids—Fundamentals of Formulation, E. Dickinson and R. Miller, eds., Royal Society of Chemistry Special Publications, London. pp. 282–292.
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, 41–49.
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. Exp. Allergy 29, 997–1004.
Richards, F.M. (1991). The protein folding problem. Sci. Am. 264, 54–62.
Riihimaki, L., Galkinab, A., Finel, M., Heikura, J., Valkonen, K., Virtanen, V., Laaksonen, R., Slotte, J.P. and Vuorela, P. (2008). Transport properties of bovine and reindeer β-lactoglobulin in the Caco-2 cell model. Int. J. Pharm. 347, 1–8.
Robillard, K.A. and Wishnia, A. (1972). Aromatic hydrophobes and β-lactoglobulin A. Kinetics of binding by nuclear magnetic resonance. Biochemistry 11, 3841–3845.
Rocha, T.L., Paterson, G., Crimmins, K., Boyd, A., Sawyer, L. and Fothergill-Gilmore, L.A. (1996). Expression and secretion of recombinant ovine β-lactoglobulin in Saccharomyces cerevisiae and Kluyveromyces lactis. Biochem. J. 313, 927–932.
Roels, H., Preaux, 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, 522–523.
Rosen, J.M., Wyszomierski, S.L. and Hadsell, D. (1999). Regulation of milk protein gene expression. Ann. Rev. Nutr. 19, 407–436.
Roufik, S., Gauthier, S.F., Leng, X.J. and Turgeon, S.L. (2006). Thermodynamics of binding interactions between bovine β-lactoglobulin A and the antihypertensive peptide β-Lg f142-148. Biomacromolecules 7, 419–426.
Rouvinen, J., Rautiainen, J., Virtanen, T., Zeiler, T., Kauppinen, J., Taivainen, A. and Mantyjarvi, R. (1999). Probing the molecular basis of allergy—three-dimensional structure of the bovine lipocalin allergen Bos-d2. J. Biol. Chem. 274, 2337–2343.
Said, H.M., Ong, D.E. and Shingleton, J.L. (1989). Intestinal uptake of retinol: enhancement by bovine milk β-lactoglobulin. Am. J. Clin. Nutr. 49, 690–694.
Sakai, K., Sakurai, K., Sakai, M., Hoshino, M. and Goto, Y. (2000). Conformation and stability of thiol-modified bovine β-lactoglobulin. Prot. Sci. 9, 1719–1729.
Sakurai, K. and Goto, Y. (2002). Manipulating monomer-dimer equilibrium of bovine β-lactoglobulin by amino acid substitution. J. Biol. Chem. 277, 25735–25740.
Sakurai, K. and Goto, Y. (2006). Dynamics and mechanism of the Tanford transition of bovine β-lactoglobulin studied using heteronuclear NMR spectroscopy. J. Mol. Biol. 356, 483–496.
Sakurai, K. and Goto, Y.J. (2007). Principal component analysis of the pH-dependent conformational transitions of bovine β-lactoglobulin monitored by heteronuclear NMR. Proc. Natl. Acad. Sci. U S A 104, 15346–15351.
Sakurai, K., Oobatake, M. and Goto, Y. (2001). Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3. Prot. Sci. 10, 2325–2335.
Sakurai, K., Konuma, T., Yagi, M. and Goto, Y. (2009). Structural dynamics and folding of β-lactoglobulin probed by heteronuclear NMR. Biochim. Biophys. Acta—Gen. Subjects 1790, 527–537.
Salier, J.P. (2000). Chromosomal location, exon/intron organization and evolution of lipocalin genes. Biochim. Biophys. Acta—Protein Struct. Mol. Enz. 1482, 25–34.
Sanchez, D., Ganfornina, M.D., Gutierrez, G., Gauthier-Juneau, A.-C., Risler, J.-L. and Salier, J.-P. (2006). Lipocalin genes and their evolutionary history, in, Lipocalins, B. Åkerström, N. Borregaard, D.R. Flower and J.-P. Salier, eds., Landes Bioscience, Georgetown. pp. 5–16.
Saufi, S.A. and Fee, C.J. (2009). Fractionation of β-lactoglobulin from whey by mixed matrix membrane ion exchange chromatography. Biotech. Bioeng. 103, 138–147.
Sawyer, W.H. (1969). Complex between β-lactoglobulin and κ-casein. A review. J. Dairy Sci. 52, 1347–1355.
Sawyer, L. (1987). One fold among many. Nature 327, 659.
Sawyer, L. (2003). β-Lactoglobulin, in, Advanced Dairy Chemistry—I Part A, 3rd edn., P.F. Fox and P.L.H. McSweeney, eds., Kluwer Academic/Plenum, New York. pp. 319–386.
Sawyer, L. and Green, D.W. (1979). The reaction of cow β-lactoglobulin with tetracyanoaurate(III). Biochim. Biophys. Acta 579, 234–239.
Sawyer, L. and Holt, C. (1993). Secondary structure of milk proteins in relation to their biological function. J. Dairy Sci. 76, 3062–3078.
Sawyer, L. and James, M.N.G. (1982). Carboxyl-carboxylate interactions in proteins. Nature 295, 79–80.
Sawyer, L. and Kontopidis, G. (2000). The core lipocalin, bovine β-lactoglobulin. Biochim.Biophys. Acta 1482, 136–148.
Schiefner, A., Chatwell, L., Breustedt, D.A. and Skerra, A. (2010). Structural and biochemical analyses reveal a monomeric state of the bacterial lipocalin Blc. Acta Crystallogr. D 66, 1308–1315.
Schlee, P., Krause, I. and Rottmann, O. (1993). Genotyping of ovine β-lactoglobulin alleles A and B using the polymerase chain-reaction. Arch. Tierzucht. 36, 519–523.
Schonfeld, D.L., Ravelli, R.B.G., Mueller, U. and Skerra, A. (2008). The 1.8Å crystal structure of α(1)-acid glycoprotein (orosomucoid) solved by UV RIP reveals the broad drug-binding activity of this human plasma lipocalin. J. Mol. Biol. 384, 393–405.
Schopen, G.C.B., Koks, P.D., van Arendonk, J.A.M., Bovenhuis, H. and Visker, M.H.P.W. (2009). Whole genome scan to detect quantitative trait loci for bovine milk protein composition. Anim. Genet. 40, 524–537.
Senti, F.R. and Warner, R.C. (1948). X-Ray molecular weight of β-lactoglobulin. J. Am. Chem. Soc. 70, 3318–3320.
Seppala, M., Koistinen, H., Koistinen, R., Hautala, L., Chiu, P.C. and Yeung, W.S. (2009). Glycodelin in reproductive endocrinology and hormone-related cancer. Eur. J. Endocrinol. 160, 121–133.
Sharma, R., Lorenzen, P.C. and Qvist, K.B. (2001). Influence of transglutaminase treatment of skim milk on the formation of ε-(γ-glutamyl)-lysine and the susceptibility of individual proteins towards crosslinking. Int. Dairy J. 11, 785–793.
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. LWT—Food Sci. Technol. 29, 763–766.
Shortle, D., Stites, W.E. and Meeker, A.K. (1990). Contributions of the large hydrophobic amino acids to the stability of staphylococcal nuclease. Biochemistry 29, 8033–8041.
Simons, J.P., McClenaghan, M. and Clark, A.J. (1987). Alteration of the quality of milk by expression of sheep β-lactoglobulin in transgenic mice. Nature 328, 530–532.
Simpson, K.J. and Nicholas, K.R. (2002). The comparative biology of whey proteins. J. Mammary Gland Biol. 7, 313–326.
Simpson, K.J., Bird, P., Shaw, D. and Nicholas, K.R. (1998). Molecular characterisation and hormone-dependent expression of the porcine whey acidic protein gene. J. Mol. Endocrinol. 20, 27–35.
Sitohy, M., Billaudel, S., Haertle, T. and Chobert, J.-M. (2007). Antiviral activity of esterified α-lactalbumin and β-lactoglobulin against herpes simplex virus type 1. Comparison with the effect of acyclovir and L-polylysines. J. Agric. Food Chem. 55, 10214–10220.
Sitohy, M., Scanu, M., Besse, B., Mollat, C., Billaudel, S., Haertle, T. and Chobert, J.-M. (2010). Influenza virus A subtype H1N1 is inhibited by methylated β-lactoglobulin. J. Dairy Res. 77, 411–418.
Skerra, A. (2008). Alternative binding proteins: anticalins—harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities. FEBS J. 275, 2677–2683.
Sostmann, K., and Guichard, E. (1998). Immobilized β-lactoglobulin on a HPLC-column: a rapid way to determine protein-flavour interactions. Food Chem. 62, 509–513.
Spector, A.A. and Fletcher, J.E. (1970). Binding of long chain fatty acids to β-lactoglobulin. Lipids 5, 403-411.
Sperber, B.L.H.M., Stuart, M.A.C., Schols, H., Voragen, A.G.J. and Norde, W. (2009). Binding of β-lactoglobulin to pectins varying in their overall and local charge density Biomacromolecules 10, 3246–3252.
Stirpe, A., Rizzuti, B., Pantusa, M., Bartucci, R., Sportelli, L. and Guzzi, R. (2008). Thermally induced denaturation and aggregation of BLG-A: effect of the Cu2+ and Zn2+ metal ions. Eur. Biophys. J. Biophys. 37, 1351–1360.
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.
Subramaniam, V., Steel, D.G. and Gafni, A. (1996). In vitro renaturation of bovine β-lactoglobulin A leads to a biologically active but incompletely refolded state. Prot. Sci. 5, 2089–2094.
Suutari, T.J., Valkonen, K.H., Karttunen, T.J., Ehn, B.-M., Ekstrand, B., Bengtsson, U., Virtanen, V., Nieminen, M. and Kokkonen, J. (2006). IgE cross reactivity between reindeer and bovine milk β-lactoglobulins in cow’s milk allergic patients. J. Invest. Allergy Clin. 16, 296–302.
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—I, P.F. Fox, ed., Applied Science Publishers, London. pp. 1–59.
Szepfalusi, Z., Loibichler, C., Pichler, J., Reisenberger, K., Ebner, C. and Urbanek, R. (2000). Direct evidence for transplacental allergen transfer. Pediatric Res. 48, 404–407.
Taheri-Kafrani, A., Gaudin, J.C., Rabesona, H., Nioi, C., Agarwal, D., Drouet, M., Chobert, J.-M., Bordbar, A.-K. and Haertlé, T. (2009). Effects of heating and glycation of β-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. J. Agric. Food Chem. 57, 4974–4982.
Takahashi, T., Yamauchi, K. and Kaminogawa, S. (1990). Comparison between the antigenicity of native and unfolded β-lactoglobulin. Agric. Biol. Chem. 54, 691–697.
Tanford, C. (1961). Physical Chemistry of Macromolecules. Wiley, New York. p. 394.
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, 1711–1715.
Tanford, C. and Taggart, V.G. (1961). Ionization-linked changes in protein conformation. II. The N-R transition in β-lactoglobulin. J. Am. Chem. Soc. 83, 1634–1638.
Tanford, C., Bunville, L.G. and Nozaki, Y. (1959). The reversible transformation of β-lactoglobulin at pH 7.5. J. Am. Chem. Soc. 81, 4032–4036.
Tatsumi, Y., Sasahara, Y., Kohyama, N., Ayano, Satomi., Endo, M., Yoshida, T., Yamada, K., Totsuka, M. and Hattori, M. (2012). Introducing site-specific glycosylation using protein engineering techniques reduces the immunogenicity of beta-lactoglobulin. Biosci. Biotechnol. Biochem. 76, 478–485.
Taulier, N. and Chalikian, T.V. (2001). Characterization of pH-induced transitions of β-lactoglobulin: ultrasonic, densimetric, and spectroscopic studies. J. Mol. Biol. 314, 873–889.
Teahan, C.G., McKenzie, H.A. and Griffiths, M. (1991). Some monotreme milk whey and blood proteins. Comp. Biochem. Physiol. B 99, 99–118.
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. Nat. Struct. Biol. 3, 863–867.
Thalmann, C.R.and Lotzbeyer, T. (2002). Enzymatic cross-linking of proteins with tyrosinase. Eur. Food Res. Technol. 214, 276–281.
The Uniprot Consortium. (2008). The Universal Protein Resource (UniProt). Nucleic Acids Res. 36(Suppl 1), D190–D195.
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, New York. pp. 109–134.
Thompson, A., Boland, M. and Singh, H. (2009). Milk Proteins—From Expression to Food. Elsevier, Amsterdam.
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., International Dairy Federation, Brussels. pp. 189–193.
Tian, F., Johnson, K., Lesar, A.E., Moseley, H., Ferguson, J., Samuel, I.D.W., Mazzini, A. and Brancaleon, L. (2006). The pH-dependent conformational transition of β-lactoglobulin modulates the binding of protoporphyrin IX. Biochim. Biophys. Acta—Gen. Subjects 1760, 38–46.
Tilley, J.M.A. (1960). The chemical and physical properties of bovine β-lactoglobulin. Dairy Science Abstr. 22, 111–125.
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. Am. Chem. Soc. 83, 464–469.
Timasheff, S.N. and Townend, R. (1964). Structure of the β-lactoglobulin tetramer. Nature 203, 517–519.
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, 2496–2501.
Timasheff, S.N., Townend, R. and Mescanti, L. (1966b). The optical rotatory dispersion of β-lactoglobulins. J. Biol. Chem. 241, 1863–1870.
Tolkach, A. and Kulozik, U. (2007). Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin. Lait 87, 301–315.
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. Am. Chem. Soc. 82, 3168–3174.
Townend, R., Weinberger, L. and Timasheff, S.N. (1960a). Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5. J. Am. Chem. Soc. 82, 3175–3179.
Townend, R., Winterbottom, R.J. and Timasheff, S.N. (1960b). Molecular interactions in β-lactoglobulin. II. Ultracentrifugal and electrophoretic studies of the association of β-lactoglobulin below its isoelectric point. J. Am. Chem. Soc. 82, 3161–3168.
Townend, R., Herskovits, T.T., Swaisgood, H.E. and Timasheff, S.N. (1964). Solution properties of β-lactoglobulin C. J. Biol. Chem. 239, 4196–4201.
Townend, R., Kumosinski, T.F. and Timasheff, S.N. (1967). The circular dichroism of variants of β-lactoglobulin. J. Biol. Chem. 242, 4538–4545.
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, 567–580.
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.
Tromelin, A. and Guichard, E. (2006). Interaction between flavour compounds and β-lactoglobulin: approach by NMR and 2D/3D-QSAR studies of ligands. Flavour Frag. J. 21, 13–24.
Ugolini, R., Ragona, L., Silletti, E., Fogolari, F., Visschers, R.W., Alting, A.C. and Molinari, H. (2001). Dimerization, stability and electrostatic properties of porcine β-lactoglobulin. Eur. J. Biochem. 268, 4477–4488.
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. Biochemistry 39, 3565–3574.
Uniacke-Lowe, T., Huppertz, T. and Fox, P.F. (2010). Equine milk proteins: chemistry, structure and nutritional significance. Int. Dairy J. 20, 609–629.
Veledo, M.T., de Frutos, M. and Diez-Masa, J.C. (2005). Analysis of trace amounts of bovine beta-lactoglobulin in infant formulas by capillary electrophoresis with on-capillary derivatization and laser-induced fluorescence detection. J. Sep. Sci. 28, 941–947.
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.
Vijayalakshmi, L., Krishna, R., Sankaranarayanan, R. and Vijayan, M. (2008). An asymmetric dimer of β-lactoglobulin in a low humidity crystal form—structural changes that accompany partial dehydration and protein action. Proteins 71, 241–249.
Vincent, F., Lobel, D., Brown, K., Spinelli, S., Grote, P., Breer, H., Cambillau, C. and Tegoni, M. (2001). Crystal structure of aphrodisin, a sex pheromone from female hamster. J. Mol. Biol. 305, 459–469.
Voet, D. and Voet, J.G. (2004). Biochemistry, 3rd edn. Wiley, New York. p. 132.
Vopel, S., Muhlbach, H. and Skerra, A. (2005). Rational engineering of a fluorescein-binding anticalin for improved ligand affinity. Biol. Chem. 386, 1097–1104.
Vyas, H.K., Izco, J.M. and Jimenez-Flores, R. (2002). Scale-up of native β-lactoglobulin affinity separation process. J. Dairy Sci. 85, 1639–1645.
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, 639–645.
Wang, Q.W., Allen, J.C. and Swaisgood, H.E. (1997). Binding of vitamin D and cholesterol to β-lactoglobulin. J. Dairy Sci. 80, 1054–1059.
Wang, Q.W., Allen, 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 J. 8, 141–148.
Warren, W.C., Hillier, L.W., Graves, J.A.M., et al. and Wilson, R.K. (2008). Genome analysis of the platypus reveals unique signatures of evolution. Nature 453, 175–183.
Watson, R.P., Demmer, J., Baker, E.N. and Arcus, V.L. (2007). Three-dimensional structure and ligand binding properties of trichosurin, a metatherian lipocalin from the milk whey of the common brushtail possum Trichosurus vulpecula. Biochem. J. 408, 29–38.
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. Nat. Struct. Biol. 5, 304–309.
Whitelaw, B. (1999). Towards designer milk. Nat. Biotech. 17, 135–136.
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, 31–39.
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. Methods 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, 375–386.
Wishnia, A. and Pinder, T.W., Jr. (1966). Hydrophobic interactions in proteins. The alkane binding site of β-lactoglobulins A and B. Biochemistry 5, 1534–1542.
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. Am. Chem. Soc. 86, 168–173.
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, 460–465.
Wu, S.Y., Perez, M.D., Puyol, P. and Sawyer, L. (1999). β-Lactoglobulin binds palmitate within its central cavity. J. Biol. Chem. 274, 170–174.
Yagi, M., Sakurai, K., Kalidas, C., Batt, C.A. and Goto, Y. (2003). Reversible unfolding of bovine β-lactoglobulin mutants without a free thiol group. J. Biol. Chem. 278, 47009–47015.
Yamada, Y., Yajima, T., Fujiwara, K., Arai, M., Ito, K., Shimizu, A., Kihara, H., Kuwajima, K., Amemiya, Y. and Ikeguchi, M. (2005). Helical and expanded conformation of equine β-lactoglobulin in the cold-denatured state. J. Mol. Biol. 350, 338–348.
Yamada, Y., Nakagawa, K., Yajima, T., Saito, K., Tokushima, A., Fujiwara, K. and Ikeguchi, M. (2006). Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine β-lactoglobulin. Proteins 63, 595–602.
Yang, M.C., Guan, H.H., Liu, M.Y., Lin, Y.-H., Yang, J.-M., Chen, W.-L., Chen, C.-J. and Mao, S.J.T. (2008). Crystal structure of a secondary vitamin D-3 binding site of milk β-lactoglobulin. Proteins 71, 1197–1210.
Yang, M.C., Chen, N.C., Chen, C.J., Wu, C.Y. and Mao, S.J.T. (2009). Evidence for β-lactoglobulin involvement in vitamin D transport in vivo- role of the γ-turn (Leu-Pro-Met) of β-lactoglobulin in vitamin D binding. FEBS J. 276, 2251–2265.
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, 243–252.
Zhang, H., Yao, J., Zhao, D., Liu, H., Li, J. and Guo, M. (2005). Changes in chemical composition of Alxa bactrian camel milk during lactation. J. Dairy Sci. 88, 3402–3410.
Zimmerman, J.K., Barlow, G.H. and Klotz, I.M. (1970). Dissociation of β-lactoglobulin near neutral pH. Arch. Biochem. Biophys. 138, 101–109.
Zsila, F. (2003). A new ligand for an old lipocalin: induced circular dichroism spectra reveal binding of bilirubin to bovine β-lactoglobulin. FEBS Lett. 539, 85–90.
Zsila, F., Imre, T., Szabo, P.T., Bikadi, Z. and Simonyi, M. (2002). Induced chirality upon binding of cis-parinaric acid to bovine β-lactoglobulin: spectroscopic characterization of the complex. FEBS Lett. 520, 81–87.
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Sawyer, L. (2013). β-Lactoglobulin. In: McSweeney, P., Fox, P. (eds) Advanced Dairy Chemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4614-4714-6_7
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