Lactoperoxidase consists of domains: a scanning calorimetric study

Thermal unfolding of lactoperoxidase (donor: hydrogen-peroxide oxidoreductase, EC 1.11.1.7) was studied by means of differential scanning calorimetry and optical methods. The protein consists of at least two domains differing in thermostability. The prosthetic group belongs to the domain of lower thermostability. Thermodynamic parameters of protein unfolding are given and found to be similar to corresponding data for globular proteins.