[Stabilization of protein by saccharose by spin marker method data]

HSA was covalently modified with maleimide spin-label. The model of label chemical exchange between inner (A) and outer (B) layers of water-protein matrix was applied. From van't-Hoff plots effective thermodynamic parameters of activation were calculated, the tendency of their alteration being found as sucrose concentration. It was revealed that sucrose induces the appearance of negative disjointing pressure. This leads to the forcing out of water layers from hydrophobic cavities in the interior of protein loosening structural flexibility and fluctuational mobility of the water-protein matrix.