Articles citing this article

The Citing articles tool gives a list of articles citing the current article.
The citing articles come from EDP Sciences database, as well as other publishers participating in CrossRef Cited-by Linking Program. You can set up your personal account to receive an email alert each time this article is cited by a new article (see the menu on the right-hand side of the abstract page).

Cited article:

Phytic acid as an efficient low-molecular-mass displacer for anion-exchange displacement chromatography of proteins

Qilie Luo and Joseph D Andrade
Journal of Chromatography B: Biomedical Sciences and Applications 741 (1) 23 (2000)
https://doi.org/10.1016/S0378-4347(00)00028-1

Effects of pH and salt environment on the association of β-lactoglobulin revealed by intrinsic fluorescence studies

D Renard, J Lefebvre, M.C.A Griffin and W.G Griffin
International Journal of Biological Macromolecules 22 (1) 41 (1998)
https://doi.org/10.1016/S0141-8130(97)00086-X

Multiple peaks in high-performance liquid chromatography of proteins ß-lactoglobulins eluted in a hydrophobic interaction chromatography system

Mercedes de Frutos, Alejandro Cifuentes and Jose Carlos Di´ez-Masa
Journal of Chromatography A 778 (1-2) 43 (1997)
https://doi.org/10.1016/S0021-9673(97)00314-2

Thermal unfolding of β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. A thermodynamic approach

Perla Relkin and D. M. Mulvihill
Critical Reviews in Food Science and Nutrition 36 (6) 565 (1996)
https://doi.org/10.1080/10408399609527740

The effect of temperature and ionic strength on the dimerisation of β-lactoglobulin

Pierre Aymard, Dominique Durand and Taco Nicolai
International Journal of Biological Macromolecules 19 (3) 213 (1996)
https://doi.org/10.1016/0141-8130(96)01130-0

Molecular basis of thermal aggregation of bovine β-lactoglobulin A

William G. Griffin, Mary C. A. Griffin, Stephen R. Martin and John Price
J. Chem. Soc., Faraday Trans. 89 (18) 3395 (1993)
https://doi.org/10.1039/FT9938903395

Gelation of globular proteins: effect of pH and ionic strength on the critical concentration for gel formation. A simple model and its application to β-lactoglobulin heat-induced gelation

D. Renard and J. Lefebvre
International Journal of Biological Macromolecules 14 (5) 287 (1992)
https://doi.org/10.1016/S0141-8130(05)80042-X

PRODUCTION OF ENRICHED PROTEIN FRACTIONS OF ?-LACTOGLOBULIN AND ?-LACTALBUMIN FROM CHEESE WHEY

C. H. AMUNDSON, S. WATANAWANICHAKORN and C. G. HILL
Journal of Food Processing and Preservation 6 (2) 55 (1982)
https://doi.org/10.1111/j.1745-4549.1982.tb00643.x

Changes in structure and hydrophobic surface properties of β-lactoglobulin determined by partition in aqueous two-phase polymeric systems

Claes-Göran Axelsson
Biochimica et Biophysica Acta (BBA) - Protein Structure 533 (1) 34 (1978)
https://doi.org/10.1016/0005-2795(78)90544-5

Thermodynamic analysis of the monomer-dimer association of .beta.-lactoglobulin A at the isoelectric point

F. J. Reithel and Michael James Kelly
Biochemistry 10 (13) 2639 (1971)
https://doi.org/10.1021/bi00789a034

Polarimetric and chromatographic investigation of the irreversible transformation of β-lactoglobulin A and B upon alkaline denaturation.

Harry Roels, Gisèle Préaux and René Lontie
Biochimie 53 (10) 1085 (1971)
https://doi.org/10.1016/S0300-9084(71)80197-9

Thermodenaturation of bovine β-lactoglobulin

W.H. Sawyer, R.S. Norton, L.W. Nichol and G.H. McKenzie
Biochimica et Biophysica Acta (BBA) - Protein Structure 243 (1) 19 (1971)
https://doi.org/10.1016/0005-2795(71)90032-8

Kinetic Studies of the Interaction of Methyl Orange with β-Lactoglobulin between pH 3.7 and 2.0

Jacques Lang, James J. Auborn and Edward M. Eyring
Journal of Biological Chemistry 246 (17) 5380 (1971)
https://doi.org/10.1016/S0021-9258(18)61918-0

The reaction of 4-(p-sulfophenylazo)-2-mercuriphenol with the thiol groups of proteins

M. Joniau, J. Bloemmen and R. Lontie
Biochimica et Biophysica Acta (BBA) - Protein Structure 214 (3) 468 (1970)
https://doi.org/10.1016/0005-2795(70)90306-5

The state of amino acid residues in β-lactoglobulin

Robert Townend, Theodore T. Herskovits, Serge N. Timasheff and Marina J. Gorbunoff
Archives of Biochemistry and Biophysics 129 (2) 567 (1969)
https://doi.org/10.1016/0003-9861(69)90216-1

Étude de l'inhibition de la protéolyse trypsique de la β-lactoglobuline a par le saccharose et quelques autres sucres. Mise en évidence d'un changement de conformation de la β-lactoglobuline a par liaison avec le saccharose

Jenny Clement-Metral and Jeannine Yon
Biochimica et Biophysica Acta (BBA) - Protein Structure 160 (3) 340 (1968)
https://doi.org/10.1016/0005-2795(68)90207-9

Exposure of Tyrosine Residues in Protein. Reaction of Cyanuric Fluoride with Ribonuclease, α-Lactalbumin, and β-Lactoglobulin*

Marina J. Gorbunoff
Biochemistry 6 (6) 1606 (1967)
https://doi.org/10.1021/bi00858a006

Étude d'une étape réversible dans la thermodénaturation de la β-lactoglobuline bovine a

Martine Dupont
Biochimica et Biophysica Acta (BBA) - Biophysics including Photosynthesis 102 (2) 500 (1965)
https://doi.org/10.1016/0926-6585(65)90140-8

Etude thermodynamique de la dissociation réversible de la β-lactoglobuline B pour des pH supérieurs à 5,5

C. Georges, S. Guinand and J. Tonnelat
Biochimica et Biophysica Acta 59 (3) 737 (1962)
https://doi.org/10.1016/0006-3002(62)90664-9