Adsorption of β-Lactoglobulin A and B in Relation to Self-Association: Effect of Concentration and pH
✍ Scribed by Elofsson, Ulla M.; Paulsson, Marie A.; Arnebrant, Thomas
- Book ID
- 120550934
- Publisher
- American Chemical Society
- Year
- 1997
- Tongue
- English
- Weight
- 182 KB
- Volume
- 13
- Category
- Article
- ISSN
- 0743-7463
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Adsorption onto chromium surfaces during heat treatment (65-68°C) of beta-lactoglobulin A and B in phosphate buffer, pH 6.88, was investigated by in situ ellipsometry. Thermal unfolding and in situ heat-induced aggregation under the same conditions were studied by differential scanning calorimetry a
milk from western cattle (16). The bovine b-lactoglobulins A description of general models for adsorption kinetics is given. are small globular proteins, and the primary structure con-Combinations of the models are compared with adsorption data sists of 162 amino acids. The A and B variants differ o
The structure of mixed A and B genetic variants of beta-lactoglobulin (beta-lg) in its native and denatured states has been studied by FTIR. The denaturation was achieved through either heating at various temperatures at pH 6 and 7 or by adsorption to the surfaces of oil droplets in oil-in-water emu