Vera A. Borzova

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Ultraviolet radiation is a risk factor for cataractogenesis. It is believed that enhanced rates of lens opacification and cataract formation are the results of gradual loss of chaperone-like efficiency of α-crystallin upon exposure to UV light. To characterize chaperone-like activity of α-crystallin damaged by UV irradiation, a test system based on(More)
A search for agents, which are capable of effectively suppressing protein aggregation, and elaboration of the appropriate test systems, are among important problems of modern biochemistry and biotechnology. One such test system is based on dithiothreitol (DTT)-induced aggregation of bovine serum albumin (BSA). Study of the kinetics of DTT-induced(More)
Thermal aggregation of bovine serum albumin (BSA) has been studied using dynamic light scattering, asymmetric flow field-flow fractionation and analytical ultracentrifugation. The studies were carried out at fixed temperatures (60°C, 65°C, 70°C and 80°C) in 0.1 M phosphate buffer, pH 7.0, at BSA concentration of 1 mg/ml. Thermal denaturation of the protein(More)
To search for agents affecting thermal stability of proteins, a test based on the registration of protein aggregation in the regime of heating with a constant rate was used. The initial parts of the dependences of the light scattering intensity (I) on temperature (T) were analyzed using the following empiric equation: I = K(agg)(T-T(0))(2), where K(agg) is(More)
The methodology for quantification of the anti-aggregation activity of protein and chemical chaperones has been elaborated. The applicability of this methodology was demonstrated using a test-system based on dithiothreitol-induced aggregation of bovine serum albumin at 45°C as an example. Methods for calculating the initial rate of bovine serum albumin(More)
Lag period is an inherent characteristic of the kinetic curves registered for protein aggregation. The appearance of a lag period is connected with the nucleation stage and the stages of the formation of folding or unfolding intermediates prone to aggregation (for example, the stage of protein unfolding under stress conditions). Discovering the kinetic(More)
Na+/K+-ATPase generates an electrochemical gradient of Na+ and K+, which is necessary for the functioning of animal cells. During the catalytic act, the enzyme passes through two ground conformational states, E1 and E2. To characterize the domain organization of the protein in these conformations, the thermal denaturation of Na+/K+-ATPase from duck salt(More)
R-phycoerithrin, a water soluble photosynthetic pigment of red algae, was used as a matrix and a reducer for the synthesis of Ag0 nanoparticles. The diameter of dominating Ag0 nanoparticles determined from the electron microscope images was 6.5 ± 0.5 nm. Dynamic light scattering in the regime of heating with a constant rate showed that the hydrodynamic(More)
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