Thermodynamic parameters of β-lactoglobulin and α-lactalbumin. A DSC study of denaturation by heating
- 20 July 1992
- journal article
- Published by Elsevier in Thermochimica Acta
- Vol. 204 (1) , 111-121
- https://doi.org/10.1016/0040-6031(92)80320-v
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- α-Lactalbumin: A calcium metalloproteinPublished by Elsevier ,2004
- Biological thermodynamic data for the calibration of differential scanning calorimeters: heat capacity data on the unfolding transition of β-lactoglobulin in solutionThermochimica Acta, 1990
- Concentration effects on the kinetics of β-lactoglobulin heat denaturation: a differential scanning calorimetric studyFood Hydrocolloids, 1990
- Enhanced thermodynamic stability of β-lactoglobulin at low pH. A possible mechanismBiochemical Journal, 1988
- Cation binding effects on the pH, thermal and urea denaturation transitions in α-lactalbuminBiophysical Chemistry, 1985
- Thermodynamics of thermal unfolding of bovine apo‐α‐lactalbuminInternational Journal of Peptide and Protein Research, 1984
- Mathematical treatment of heat flow in differential scanning calorimetry and differential thermal analysis instrumentsReview of Scientific Instruments, 1982
- Thermodynamics of α-lactalbumin unfoldingBiophysical Chemistry, 1981
- Thermal Stability of β-Lactoglobulin as a Function of pH and the Relative Concentration of Sodium DodecylsulphateActa Agriculturae Scandinavica, 1980
- Stability of Proteins Small Globular ProteinsAdvances in Protein Chemistry, 1979