[Efficacy of adepress (paroxetine) in the treatment of depression in patients with chronic cerebral ischemia in the late recovery phase of ischemic stroke with the estimation of the velocity of passive transmembrane ion transport].

We studied the correlation between the efficacy of adepress (paroxerine) and the state of cell membranes assessed by the velocity of passive transmembrane ion transport in 39 patients (20 patients with chronic brain ischemia and 19 patients with ischemic stroke). Velocity of passive transmembrane ion transport estimated by the level of Na+-Li+ counter-transport (NLC) in the erythrocyte membrane was a criterion of the cell membrane functional activity. The higher the NLC velocity, the more severe was the course of depression with the development of cognitive dysfunction and pain syndromes in patients with chronic brain ischemia and stroke. At the same time, the higher clinical efficacy of adepress (paroxerine) was seen in patients with higher NLC velocities. Estimation of NLC velocity in the erythrocyte membrane may be used for identification of risk groups for the development of affective disorders in patients with stroke and chronic brain ischemia as well as for prediction of treatment efficacy.

[Kinetics of fibrin lysis by plasmin: inhibition by fibrin degradation products]. / Kinetika lizisa fibrina plazminom: ingibirovanie produktami degradatsii fibrina.

A kinetics of lysis of 125I-labeled fibrin coagulates by plasmin was studied. The strong competitive inhibition of fibrinolysis by the products of fibrin degradation was found. On the basis of the integral analysis of the complete kinetic curves of the fibrinolysis products accumulation, the Michaelis constant Km, the catalytic constant of the reaction of fibrinolysis by plasmin kcat, and the constant of inhibition by the reaction products Ki were determined to be 1.3 microM, 1.36 min-1, and 0.12 microM, respectively. The results obtained showed that the efficiency of plasmin inhibition by the reaction products exceeds that of plasmin interaction with the substrate. Thus, the process of fibrinolysis is regulated by a negative feedback mechanism.

[Binding of an acylated plasminogen activator-streptokinase complex with fibrin and the fibrinolytic response in vitro]. / Sviazyvanie atsilirovannogo aktivatornogo kompleksa plazminogen-streptokinaza s fibrinom i fibrinoliticheskii otvet in vitro.

Affinity and fibrinolytic properties of streptokinase and two new preparations of acylated plasminogen-streptokinase activator complexes, produced by dissimilar procedures, were studied. Even after 1-min exposure, blood clot lysis carried out by the acyl activating complex was continued in blood plasma more than for 4 hrs, while the streptokinase produced blood clot lysis was accomplished within 1.5 hrs. After 1-min contact with clot in blood plasma the rates of lysis by streptokinase and these acylated plasminogen-streptokinase activator complexes types 1 and 2 constituted 23%, 37% and 63%, respectively, as compared with the rates detected during permanent contact of thrombolytics with blood clot. The activator properties of the thrombolytic agents itself and its stability in blood plasma were of importance even in similar affinity ability of free and acylated activating complexes.

[The thrombolytic activity of acylated activator complexes of plasmin-streptokinase with different rates of reactivation]. / Tromboliticheskaia aktivnost' atsilirovannykh aktivatornykh kompleksov plazmin--streptokinaza s razlichnymi skorostiami reaktivatsii.

In the experiments on guinea-pigs with venous thrombosis there were studied the fibrin- and thrombolytic effects of streptokinase, the plasmin-streptokinase complex and the acylated derivatives of the complex with various rates of reactivation. It was established that the acylated derivatives of the plasmin-streptokinase complex possess greater stability in the blood flow and lead to more prolonged stimulation of fibrinolysis at less magnitude of its systemic activation. Due to this the acylated derivatives of the plasmin-streptokinase complex produce less pronounced fibrinogenolysis. In connection with a high affinity to fibrin their thrombolytic action does not depend on the systemic activation of fibrinolysis.

[Kinetics of in vitro fibrinolysis by plasmin and a plasmin-streptokinase equimolar complex]. / Kinetika fibrinoliza in vitro plazminom i ékvimoliarnym kompleksom plazmin-streptokinaza.

Kinetics of fibrinolysis by plasmin and plasmin streptokinase complex have been studied using fibrin gels formed from purified fibrin and human blood plasma. The gels were placed into buffer or blood plasma. The contributions of plasminogen and alpha 2-antiplasmin present or absent in both phases to the kinetics of fibrinolysis were quantitatively estimated. In the complex catalyzed fibrinolysis, plasminogen activation reaction dominated whereas in plasmin-catalyzed fibrinolysis, the inhibitor involved reaction, suppressing the process, prevailed.

[Catalytic properties of plasmin and the equimolar plasmin-streptokinase complex in their reactions with various substrates and inhibitors]. / Kataliticheskie svoistva plazmina i ékvimoliarnogo kompleksa plazmin-streptokinaza v reaktsiiakh s razlichnymi substratami i ingibitorami.

The interactions of plasmin and plasmin-streptokinase equimolar complex with a number of protein and low-molecular weight substrates as well as protein inhibitors have been examined. It was concluded that the above interactions entail structural changes in the complexes formed, which trigger the activator, increase the rate constants of low molecular weight substrates but create steric hindrances to the interaction with protein substrates and inhibitors.