S. D. Razumovskii

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The mechanism of self-assembly of fibrin monomers and fibrinogen aggregation during ozone oxidation has been studied by the methods of elastic and dynamic light-scattering and viscosimetry. Fibrin obtained from oxidized fibrinogen exhibits higher average fiber mass/length ratio compared with native fibrin. Fibrinogen ozonation sharply reduced the latent(More)
Oxidation of arachidonic acid by ROS in vitro can be evaluated by the formation of reaction products (conjugated dienes); this is preceded by a lag period caused by the action of antioxidants (α-tocopherol, β-carotene, and ascorbic acid). In case of ozone titration the oxidizer is consumed even during the lag period, when conjugated dienes are not yet(More)
Ozone-induced free-radical oxidation of fragments D and E from fibrinogen has been studied. The methods of elastic and dynamic light scattering in combination with electrophoresis of unreduced samples have shown the acceleration of enzymatic covalent crosslinking of molecules of oxidation-modified fragment D under the action of factor XIIIa. UV and IR(More)
213 Fibrin stabilizing factor (FXIII) belongs to the family of transglutaminases (endo γ glutamine:ε lysine transferase, EC. 2.3.2.13) and is one of the key proteins of the blood coagulation system. Similarly to other blood clotting factors, FXIII circulates in plasma as an inactive precursor. This is a heterotet ramer (FXIII A2B2) with a molecular weight(More)
Using an original automated analyzer of double bonds we determined the rate constants for oxidation of saturated and unsaturated mono- and dienoic fatty acids (in vivo substrates for β-oxidation in the mitochondria) by the ozone titration method. The rate constant for O3 oxidation is maximum for oleic monoenoic acid, lower for dienoic linoleic, and very low(More)
The mechanism of enzymatic covalent crosslinking of fibrinogen molecules under the effect of plasma transglutaminase (factor XIIIa) has been studied. Using the methods of elastic and dynamic light scattering combined with viscosimetry and electrophoresis of the reduced samples, it has been shown that fibrinogen oxidation strongly accelerates self-assembly(More)
, H2O2, etc. [1, 2]. In some cases, these secondary ROS can be even more deleterious than the ozone molecules themselves. It is now generally recognized that proteins are among the main targets of ROS. Under the action of ROS, proteins undergo oxidative modifications, which disturb their structures and functions. Oxidation modified proteins accumulate in(More)
The ability of dihydroquercetin to inhibit the oxidation of fibrinogen has been evaluated. It is established that dihydroquercetin inhibits oxidation of fibrinogen by ozone, thus preventing oxidative modification of fibrinogen and preserving its functional activity.
The ability of a water-soluble inclusion complex (KN-14-CD) of an aminomethylated dihydroquercetin derivative (KN-14) in β-cyclodextrin (CD) to inhibit ozone-induced oxidation of fibrinogen was evaluated. KN-14-CD prevented ozone-induced oxidation of fibrinogen and preserved its ability to form clots after the addition of thrombin. The ability of KN-14-CD(More)
20 Fibrinogen is a multidomain blood plasma protein, the main function of which is to produce insoluble fibrin. Fibrinogen molecule is a dimer comprised of three pairs of polypeptide chains ( A α , B β , and γ ) 2 . The central part of the molecule, encompassing the NH 2 terminal regions of all polypeptide chains, forms the central domain E , which contains(More)