The effect of temperature and ionic strength on the dimerisation of β-lactoglobulin
- 1 October 1996
- journal article
- Published by Elsevier in International Journal of Biological Macromolecules
- Vol. 19 (3) , 213-221
- https://doi.org/10.1016/0141-8130(96)01130-0
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- A Comparison of the Structure of β-Lactoglobulin Aggregates Formed at pH7 and pH2International Journal of Polymer Analysis and Characterization, 1996
- Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperatureBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1988
- 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 proteinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1985
- Particle diffusion as a function of concentration and ionic strengthThe Journal of Physical Chemistry, 1978
- Molecular Interactions in β-Lactoglobulin. X. The Stoichiometry of the β-Lactoglobulin Mixed Tetramerization1Journal of the American Chemical Society, 1966
- Crystal forms of β-lactoglobulinJournal of Molecular Biology, 1965
- Molecular Interactions in β-Lactoglobulin. VI. the Dissociation of the Genetic Species of β-Lactoglobulin at Acid pH's2Journal of the American Chemical Society, 1961
- Molecular Interactions in β-Lactoglobulin. IV. The Dissociation of β-Lactoglobulin below pH 3.52Journal of the American Chemical Society, 1960
- Molecular Interactions in β-Lactoglobulin. III. Light Scattering Investigation of the Stoichiometry of the Association between pH 3.7 and 5.22Journal of the American Chemical Society, 1960
- The Specific Refractive Increment of Some Purified ProteinsJournal of the American Chemical Society, 1948