[Thermal denaturation of oligomeric proteins: structural and functional modifications, the sequence of steps].

On the basis of literature and own experimental data changes in the structural and functional properties of some oligomeric proteins of the blood system (hemoglobin, lactate dehydrogenase, superoxide dismutase, catalase) exposed to the influence of temperature in a broad range were analyzed. The many-phase character of the temperature modification of protein molecules with different values of functional and kinetic parameters for each of revealed stages was discovered. At a critical temperature and at higher values, the dissociation of oligomeric proteins into separate subunits was shown to occur along with the typical "loosening" of the protein globule. It was shown that low-molecular components (subunits) can subsequently associate with one another and with oligometic proteins, which leads to irreversible denaturation and to the unusual physicochemical behavior of protein molecules. Schemes of processes underlying the temperature modifications of the proteins studied were elaborated.