Article
Thermodynamic characterization of the partially unfolded state of Ca(2+)-loaded bovine alpha-lactalbumin: evidence that partial unfolding can precede Ca2+ release.
Biochemistry - 24 Dec 1996
Vanderheeren G, Hanssens I, Meijberg W, Van Aerschot A
Abstract excerpt
The thermal denaturation of bovine alpha-lactalbumin (BLA) was studied at pH 7.5 and at various Ca2+ concentrations using near-UV circular dichroism and differential scanning calorimetry. The Ca2+ dependence of the denaturation equilibria proves that, in the transition region, partially unfolded...
Topics
- Animals
- Binding Sites
- Calcium
- Calorimetry, Differential Scanning
- Cattle
- Circular Dichroism
- Humans
- Hydrogen-Ion Concentration
- In Vitro Techniques
- Lactalbumin
- Muramidase
- Mutation
- Protein Conformation
- Protein Denaturation
- Protein Folding
- Recombinant Proteins
- Thermodynamics