BETA LACTOGLOBULIN BIBLIOGRAPHY

. Beta- lactoglobulin is the major whey protein in the milk of ruminants and some nonruminants. It was first isolated 60 years ago and a wealth of physico-chemical and biological information has been accumulated.
The amino acid sequences have been determined for b-lactoglobulins of several species and several DNA sequences and gene structures have been reported. The conformational structure of b-lactoglobulin has been studied by x-ray crystallography. The core of the molecule is made up of a very short a-helix segment and eight strands of anti-parallel b-sheet, which wrap round to form an antiparallel b-barrel. An interesting physico-chemical property of b-lactoglobulin is its ability to bind in vitro small hydrophobic substances such us retinol and fatty acids.

THIS REFERENCES FILE IS MAINTAINED BY DOLORES PEREZ, E-MAIL dperez@mvet.unizar.es
Comments and contributions are welcomed


Alexander L.J., Hayes G., Pearse M.J., Beattie C.W., Stewart A.F., Willis L.M. y Mackinlay A.G. (1989) Complete sequence of the bovine b-lactoglobulin cDNA. Nucleic Acids Res. 17, 6739.

Ali S. y Clark J. (1988) Characterization of the gene encoding ovine beta-lactoglobulin. Similarity to the genes for retinol binding protein and other secretory proteins. J. Mol. Biol. 199, 415-426.

Armstrong J.M. y Mckenzie H.A. (1967) A method for modification of carboxyl groups in proteins: its application to the association of bovine b-lactoglobulin A. Biochim. Biophys Acta 147, 93-99.

Armstrong J.M. y Mckenzie H.A. y Sawyer W.H. (1967) On the fractionation of b-lactoglobulin and a-lactalbumin. Biochim. Biophys Acta 147, 60-72.

Aschaffenburg R. y Drewry J. (1955) Occurrence of different beta-lactoglobulins in cow's milk. Nature 176, 218-219.

Aschaffenburg R. y Drewry J. (1957) Genetics of the b-lactoglobulins of cow's milk. Nature 180, 376-377.

Aschaffenburg R. y Drewry J. (1957) Improved method for the preparation of crystalline b-lactoglobulin and a-lactalbumin. from cow's milk. Biochem. J. 65, 273-277.

Asselin J., Hebert J. y Amiot J. (1989) Effects of in vitro proteolysis on the allergenicity of major whey proteins. J. Dairy Sci. 54, 1037-1039.

Bash J.J. y Timasheff S.N. (1967) Hydrogen ion equilibria of the genetic variants of bovine b-lactoglobulin. Arch. Biochem. Biophys. 118, 37-47.

Bastian,E.D; Hansen,K.G; Brown,R.J (1993) Inhibition of plasmin by beta-lactoglobulin using casein and a synthetic substrate. J. Dairy Sci, 1993, 76(11): 3354-3361.

Beckerdite J.M., Weirich C.A. y Adams E.T. (1983) Sedimentation coefficients of self-associating species. II. Tests with a simulated example and with b-lactoglobulin A. Biophys. Chem. 17, 203-210.

Bell K. (1967) The detection and occurrence of bovine b-lactoglobulin C. Biochim. Biophys. Acta 147, 100-108.

Bell K. Mckenzie H.A. y Shaw D.C. (1981) Porcine b-lactoglobulin A and C. Mol. Cell. Biochem. 35, 103-111.

Bell K. y Mckenzie H.A. (1964) b-lactoglobulins. Nature 204, 1275-1279.

Bell K. y Mckenzie H.A. (1967) The isolation and properties of bovine b-lactoglobulin C. Biochim. Biophys. Acta 147, 109-122.

Bell K. y Mckenzie H.A. (1967) The whey proteins of ovine milk: b-lactoglobulins A and B. Biochim. Biophys. Acta 147, 123-134.

Bell K., Mckenzie H.A., Murphy W.H. y Shaw D.C. (1970) b-lactoglobulin droughtmaster: a unique protein variant. Biochem. Biophys. Acta 214, 427-436.

Brand E., Saidel J.J.,Goldwater W.H., Kaseel B. y Ryan F.J. (1945) The empirical formula of b-lactoglobulin. J.Am. Chem. Soc. 67, 1524-1532.

Braunitzer G., Chen R., Schrank B. y Stangl A. (1972) Automatishe sequenzanalyse eines proteins (b-lactoglobulin AB). Hoppe-Seyler's Z. Physiol. Chem. 353, 832-834.

Braunitzer G., Chen R., Schrank B. y Stangl A. (1973). Die sequenzanalyse des b-lactoglobulins. Hoppe-Seyler's Z. Physiol. Chem. 354, 867-878.

Brignon G. y Ribadeau-Dumas B. (1973) Localisation dans la chaine peptidique de la b-lactoglobuline bovine de la substitucion Glu-Gln differenciant les variants genetiques B et D. FEBS Lett. 33, 73-76.

Brignon G., Chtorou A. y Ribadeu-Dumas B. (1985) Does b-lactoglobulin occur in human milk. J Dairy Res. 52, 249-254.

Brown E.M. (1984) Interactions of b-lactoglobulin and a-lactalbumin with lipids: a review. J. Dairy Sci. 67, 713-722.

Brown E.M., Carroll R.J., Pfeffer P. y Sampugna J. (1983) Complex formation in sonicated mixtures of b-lactoglobulin and phosphatidylcholine. Lipids 18, 111-118.

Caffin J.P., Poutrel B. y Rainard P. (1985) Physiological and pathological factors influencing bovine a-lactalbumin and b-lactoglobulin concentration in milk. J. Dairy Sci. 68, 1087-1094.

Caillard,I; Tome,D (1994) Modulation of beta-lactoglobulin transport in rabbit ileum. Am. J. Physiol. 266(6 PART 1): G1053-G1059

Cairoli,S; Iametti,S; Bonomi,F. (1994) Reversible and irreversible modifications of beta-lactoglobulin upon exposure to heat. J. Prot. Chem.13(3): 347-354

Cannan R.K., Palmer A.H. y Kibrick A.C. (1942) The hydrogen ion dissociation curve of b-lactoglobulins. J. Biol. Chem. 142, 803-822.

Cauvin E., Conti A. y Liberatori J. (1977) Comparative structural studies on b-lactoglobulins. The N-terminal sequence of sheep, goat and buffalo b-lactoglobulins. Milchwissenschaft 32, 459-460.

Chen, S.X; Hardin,C.C; Swaisgood,H.E (1993) Purification and characterization of beta-structural domains of beta-lactoglobulin liberated by limited proteolysis. J. Protein Chem, 12(5): 613-625

-Chen, S.X; Swaisgood, H.E; Foegeding,E.A Gelation of beta-lactoglobulin treated with limited proteolysis by immobilized trypsin. Journal of Agricultural and Food Chemistry , 1994,42(2): 234-239

Cho,Y; Gu,W; Watkins,S; Lee,S.P; Kim,T.R; Brady,J.W; Batt,C.A (1994) Thermostable variants of bovine beta-lactoglobulin. Prot. Engin., 7(2): 263-270

Conti A., Godovac-Zimmermann J. Pirchner F., Liberatori L. y Braunitzer G. (1986) Pig b-lactoglobulin I (Sus scrofa domestica, Artiodactyla). Biol. Chem. Hoppe-Seyler 367, 871-878.

Conti A., Godovac-Zimmermann J., Liberatori L. y Braunitzer G. (1986) Preparative separation of pig polymorphic beta-lactoglobulin by IPG and non-IPG. Prot. Biolog. Fluids Proc. Colloq. 34, 907-910.

Conti A., Godovac-Zimmermann J., Liberatori L., Braunitzer G. y Minori D. (1984) The primary structure of monomeric b-lactoglobulin I from horse colostrum (Equus caballus, Perisodactyla). Hoppe-Seyler's Z. Physiol. Chem. 365, 1393-1401.

Conti A., Liberatori J. y Napolitano L. (1980) Isolation and preliminary physico-chemical characterization of human b-lactoglobulin. Milchwissenschaft 35, 65-68.

Conti A., Liberatori J. y Napolitano L. (1982) Heterogeneity of equine b-lactoglobulins. Milchwissenschaft 37, 338-340.

Conti A., Napolitano L., Cantisani A.M., Davoli R. y Dall'Ollio S., (1988) Bovine b-lactoglobulin H: isolation by preparative isoelectric focusing in immobilized pH gradients and preliminary characterization. J. Biochem. Biophys. Met. 16, 205-214.

Conti A., Napolitano L., Lai P., Pinna W. y Godovac-Zimmermann J. (1989) Isolation of donkey whey proteins and N-terminal amino acid sequence of a-lactalbumins A and B, b-lactoglobulins I and II and lysozyme. Milchwissenschaft 44, 138-141..

Cornell D. G. (1982) Lipid-protein interactions in monolayers: egg yolk phosphatidic acid and b-lactoglobulin. J. Coll. Interface Sci. 88, 536-545.

Cornell D.G. y Patterson D.L. (1989) Interaction of phospholipids with b-lactoglobulin adsorbed from solution. J. Agric. Food Chem. 37, 1455-1459.

Creamer L.K., Parry D.A.D. y Malcolm G.N. (1983) Secondary structure of bovine b-lactoglobulin. Arch. Biochem. Biophys. 227, 98-105.

Diaz de Villegas M.C., Oria R., Sala F.J. y Calvo M. (1987) Lipid binding by b-lactoglobulin of cow milk. Milchwissenschaft. 42, 357-358.

Dickinson, E (1994) Protein-stabilized emulsions. J. Food Engineer. 22(1-4): 59-74

Dodd, S.C; Forsyth, I.A; Buttle, H.L; Gurr, M.I; Dils, R.R (1994) Hormonal induction of alpha-lactalbumin and beta-lactoglobulin in cultured mammary explants from pregnant pigs. J. Dairy Res., 61(1): 35-45

Doi H., Ibuki F. y Kanamori M.(1981) Effect of carbohydrate moiety of K-casein on the complex formation with b-lactoglobulin. Agric. Biol. Chem. 45, 2351-2353.

Doi H., Ideno S., Ibuki F. y Kanamori M. (1983) Participation of the hydrophobic bond in complex formation between K-casein and b-lactoglobulin. Agric. Biol. Chem. 47, 407-409.

Doi H., Ideno S., Kuo F.H., Ibuki F. y Kanamori M. (1983) Gelation complex between K-casein and b-lactoglobulin. J. Nutr. Sci. Vitaminol. 29, 679-689.

Dufour, E; Dalgalarrondo, M; Haertle, T. (1994) Limited proteolysis of beta-lactoglobulin using thermolysin: Effects of calcium on the outcome of proteolysis. Int. J. Biol.Macromol., 16(1): 37-41

Dufour, E; Genot, C; Haertle, T (1994) Beta-Lactoglobulin binding properties during its folding changes studied by fluorescence spectroscopy. Biochim. Biophys. Acta, 1205(1): 105-112.

Dufour, E; Hoa, G.H.B; Haertle,T. (1994) High-pressure effects on beta-lactoglobulin interactions with ligands studied by fluorescence. Biochimica et Biophysica Acta 1206(2): 166-172


Dufour, E; Robert, P; Bertrand, D; Haertle, T (1994) Conformation changes of beta-lactoglobulin: An ATR infrared spectroscopic study of the effect of pH and ethanol. Journal of Protein Chemistry 13(2): 143-149


Dufour,E; Haertle,T (1993) Temperature-induced folding changes of beta-lactoglobulin in hydro-methanolic solutions. Int. J. Biol.Macromol 15(5): 293-297

Dunnill P. y Green D.W. (1965) Sulphydryl groups and the N-R conformotional change in b-lactoglobulin. J. Mol. Biol. 15, 147-151.

Ena J.M., Castillo H., S‡nchez L. y Calvo M. (1990) Isolation of human lactoferrin by affinity chromatography using insolubilized bovine b-lactoglobulin. J. Chromat. 525, 442-446.

Erhardt G. (1989) Evidence for a third allele at the b-lactoglobulin locus of sheep milk and its occurrence in different breeds. An. Genet. 20, 197-204.

Erhdart G., Godovac-Zimmermann J. y Conti A. (1989) Isolation and complete primary sequence of a new ovine wild-type b-lactoglobulin C. Biol. Chem. Hoppe-Seyler 370, 757-762.

Farrel H.M., Behe M.J. y Rnyeart J.A. (1987) Binding of p-nitrophenyl phosphate and other aromatic compounds by b-lactoglobulin. J. Dairy Sci. 70, 252-258.

Folch J.M., Coll A. and Sanchez A. (1993) Cloning and sequencing of the cDNA encoding goat beta-lactoglobulin. J. Anim Sci. 71, 2832

Folch J.M., Coll A. and Sanchez A. (1994) Complete sequence of the caprine beta-lactoglobulin gene. J. Dairy Sci 77, 3493-3497

Folch J.M., Coll A. Hayes H.C. and Sanchez A. (1996) Characterization of caprine beta-lactoglobulin pseudogene, identification and chromosomal localization by in situ hybridization in goat, sheep and cow. Gene

Frick M. and Rieger C.H.L. (1987) Local antibodies to a-casein and b-lactoglobulin in the saliva of infants. Pediatr. Res. 22, 399-401.

Fugate R.D. and Song P. (1980) Spectroscopic characterization of b-lactoglobulin-retinol complex. Biochim. Biophys. Acta 625, 28-42.

Futterman S. y Heller J. (1972) The enhancement of fluorescence and the decreased susceptibility to enzimatic oxidation of retinol complexed with bovine serum albumin, b-lactoglobulin and the retinol-binding protein of human plasma. 247, 5168-5172.

Gaye P., Hue-Delahaie D., Mercier J.C., Soulier S., Vilotte J.L. y Furet J.P. (1986) Ovine b-lactoglobulin messenger RNA: nucleotide sequence and mRNA levels during functional differentiation of the mammary gland. Biochimie 68, 1097-1107.

Gaye P., Viennot N. y Denamur R. (1972) In vitro synthesis of a-lactalbumin and b-lactoglobulin by microsomes and bound polyribosomes from the mammary gland of lactating sheep. Biochim. Biophys. Acta 262, 371-380.

Ghose A.C., Chaudhuri S. y Sen A. (1968) Hydrogen Ion Equilibria and Sedimentation behavior of goat b-lactoglobulin. Arch. Biochem. Biophys. 126, 232-243.

Godovac-Zimmermann J. (1988) The structural motif of b-lactoglobulin and retinol-binding protein: a basic framework for binding and transport of small hydrophobic molecules?. Trends. Biochem. Sci. 13, 64-67.

Godovac-Zimmermann J. y Braunitzer G. (1987) Modern aspects of the primary structure and function of b-lactoglobulins. Milchwissenschaft 42, 294-297.

Godovac-Zimmermann J. y Shaw D. (1987) The prymary estructure, binding site and possible function of b-lactoglobulin from Eastern Grey Kanguroo (Macropus giganteus). Biol. Chem. Hoppe-Seyler, 368, 879-886.

Godovac-Zimmermann J., Conti A., James L. y Napolitano L. (1988) Microanalysis of the amino-acid sequence of monomeric b-lactoglobulin from Donkey (Equus asinus) milk. Biol. Chem. Hoppe-Seyler 369, 171-179.

Godovac-Zimmermann J., Conti A., Liberatori J. y Braunitzer G. (1985) Homology between the primary structures of b-lactoglobulins and human retinol-binding protein: evidence for a similar biological function?. Biol. Chem. Hoppe-Seyler. 366, 431-434.

Godovac-Zimmermann J., Conti A., Liberatori J. y Braunitzer G. (1985) The aminoacid sequence of b-lactoglobulin II from horse colostrum (Equus caballus, Perisodactyla): b-lactoglobulins are retinol-binding proteins. Biol. Chem. Hoppe-Seyler 366, 601-608.

Godovac-Zimmermann J.,Conti A. y Napolitano L. (1987) The complete amino-acid sequence of dimeric b-lactoglobulin from mouflon (ovis ammon musimon) milk. Biol. Chem. Hoppe-Seyler 368, 1313-1319.






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