Biomedical subjects
Publications and source records attributed to L I Sokolovskaia.
A physical model of the kinetics of the fibrinogen--fibrin transition was constructed using the theory of phase transitions. It was shown that the model is consistent with the experimental data.
The function of lysine-binding sites in kringle domains K1-4 and K5 of plasminogen (Pg) during its activation by streptokinase (SK) was studied. Activation rates of Glu- and Lys-Pg exceed activation rate of mini- and micro-Pg 26 and 40 times, respectively. 6-Animohexanoic acid (6-AHA) in concentrations from 10(-5) to 10(-2) M inhibits activation of Glu-, Lys- and mini-Pg and does not impact the activation of micro-Pg. Complete inhibition of Lys-Pg activation occurs with presence of 10(-3) M 6-AHA while 90% inhibition of mini-Pg activation and 70% inhibition of Glu-Pg activation occur with 10(-2) M 6-AHA. Isolated kringles K1-3 and K4 of Pg inhibit activation of Glu-Pg by SK and concentrations [I]50 are 4.0 and 8.1 x 10(-6) M, respectively. Catalytic activity of Glu-Pg-SK, Lys-Pg-SK and Pm-SK complexes with respect to S 2251 is not inhibited by 6-AHA in concentrations from 10(-5) to 10(-2) M. Activation of substrate Pg by Pm-SK complex is also inhibited by 6-AHA in concentrations from 10(-5) to 10(-2) M; however, this effect of inhibition is significantly weaker than that with activation by SK. Cleavage of C-terminal Lys or chemical modification of NH2-groups of amino acid residues in SK molecule also results in the decrease of the Glu-Pg activation rate. Lysin-binding sites in K1-4 and K5 of Pg molecule are important at different steps of Pg activation process which includes formation of equimolar complex; structural reorganizations resulted in formation of active center in Pg; and binding of substrate Pg with Pg-SK complex. Lysin-binding sites in K1-4 of Pg are necessary for maintenance of high rate of Pg activation by SK.
Dependence of fibrinolysis parameters on the concentration of inhibitors of fibrinolytic process has been studied when using turbidimetric method. It is shown that the process of destruction of fibrin clot formed in diluted blood plasma is subjected to the Michaelis-Menten ratio. The constant of inhibition of fibrinolytic process in diluted plasma activated by prothrombin and streptokinase is 10 and 0.5 microM for 6-aminohexanoic acid and contrykal, respectively.
A method has been developed to determine six parameters of coagulation and fibrinolysis by means of turbidimetry; 0.1 ml of dissolved plasma after its activation with thrombin and streptokinase is used. Testing conditions which permit performing express diagnostics of haemostasis disturbances and controlling their correction have been optimized.
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