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Biomedical subjects

E S Zhitnikova

Publications and source records attributed to E S Zhitnikova.

14 recordsLinked to original sources
PubMed1983

[Electron microscopic study of the depolymerization process on unstabilized fibrin as affected by urea or monochloracetic acid].

With the help of the electronmicroscopic method the non-stabilized fibrin depolymerization has been studied. It has been established that under the action of urea or monochloridacetic acid the gradual transition of fibril clot's structure in globular fibrinolike material takes place. These globules have morphological likeness with the fibrin-monomer molecules and have analogy of the morphological properties to the non-stabilized fibrin dissolution products by complex compounds of heparin. The elimination of urea or monochloridacetic acid from media gives possibility to reconstruct the fibrillar fibrin structure.

Acetates↗
PubMed1978

[Ultrastructure of unstabilized fibrin].

The structure of non-stabilized fibrin was studied by electron microscopy. Non-stabilized fibrin was shown to consist of a network of fibers (fibrils, from 2 to 10 mu in length, and up to 200 A in width). Negative contrasting with uranyl-acetate demonstrated non-stabilized fibrils to be made up of 5 to 10 longitudinally striated protofibrils and to be characterized by transverse striations with the main period of about 200 A. Comparison of the ultrastructure of stabilized and non-stabilized with factor XIIIa fibrin fibers demonstrated their morphological affinity.

Animals↗
PubMed1978

[Electron microscopic study of the products from dissolving unstabilized fibrin with complex heparin compounds].

Effects of some heparin complex compounds (heparin-urea, adrenaline-heparin, fibrinogen-heparin complexes and secondary complex adrenalin-heparin-fibrinogen) on factor XIIIa unstabilized fibrin were studied using electron microscopy. Fibrillar network of unstabilized fibrin destroys with the formation of globular molecular particles similar to fibrinogen molecule or fibrin monomer ultrastructure. A mechanism of fibrinolytic action of all the complexes mentioned is probably the same, since under dissolving of unstabilized fibrin, structures are found, which are similar to those forming under dissolving of unstabilized fibrin with urea.

Chemical Phenomena↗
PubMed1977

[Fibrinolysis in several organs following splenectomy in animals].

Spleenectomy was found to have a disturbing effect on the anticoagulating system (ACS) function and to elicit changes of the fibrinolytic activity in tissues of some organs. At the greatest ACS suppression, on the 7th day after spleenectomy, the animals had a decreased total fibrinolytic activity (TFA) in extracts from the liver and lungs, while the activity was utterly absent in extracts from the heart. By the end of the restoration period of ACS function, on the 21st day after the surgery, in experimental animals no fibrinolysis was revealed in the extract from the myocardium, neither the unfermentative fibrinolysis (UF) was observed in extracts from the liver and lungs. Simultaneously a considerable fibrinolytic activity occurred in the tissues of kidneys and thymus, mainly on account of UF. Evidently, after spleenectomy the biosynthesis and accumulation of agents exerting unfermentative fibrinolytic activity is transferred from some organs to others.

Animals↗
PubMed1976

[Changes in the functioning of the anticoagulant system of splenectomized animals during immobilization].

Changes of the anticoagulating system's (ACS) function depend on time elapsing after removal of the spleen, therefore different degrees of ACS activation after 30-min immobilization stress can be observed. In the animals with completely or partially removed spleen, the stress induces activation of the ACS function as expressed by increase in the plasma total fibrinolytic activity, nonfermentative fibrinolysis, decrease in the fibrinogen concentration, activation of the blood plasma anticoagulating function. Hovewer, on the 7th--9th day after removal of the spleen, when the ACS function is thoroughly depressed, the 30-min immobilization stress decreases the plasma anticoagulating activity and, to a certain extent, restricts the appearance of the heparin complex compounds. The latter is due to antagonistic effect of the factor XIII whose activity increases in the blood of the experimental animals. By the 21st day a complete restoration of ACS function occurs in the spleenectomized animals which accounts for the same degree of ACS activation in response to the stress both in the experimental and in control animals.

Animals↗
PubMed1976

[The anticoagulant system following intravenous administration of factor XIII and thromboplastin].

The inactivated factor XIII does not change the functional state of the anticoagulating system. The i.v. administration of thromboplastin activates the anticoagulating system in rats which cannot be prevented by an artificial rise of the titre of the inactivated factor XIII in blood. The i.v. injections of the secondary adreanlin-heparin--fibrinogen complex with higher level of the factor XIII is followed by a sharp increase in the functional activity of the anticoagulating system.

Animals↗
PubMedDate not supplied

[Formation of a secondary adrenaline-heparin-fibrinogen complex and its properties].

An effect of increase in fibrinolytic activity of adrenaline-heparin (ADH) complex was studied under its incubation in a mixture with pure fibrinogen on unstablized plates of fibrin in presence of xi-aminocapronic acid, By means of spectrophotometry in UV-light an increase in lytic activity of the incubated mixture of adrenaline-heparin complex with fibrinogen was shown to be due to formation of a secondary complex, which included adrenaline, heparin and fibrinogen. After intravenous administration of a mixture of ADH complex with fibrinogen, containing products of interaction of adrenaline, heparin and fibrinogen, not only an increase in non-enzymic fibrinolytic activity of plasma occurred, but also an increase in duration of an effect of adrenaline--heparin--fibrinogen complex was observed in vivo as compared with the equivalent dose of the ADH complex

Aminocaproates↗
PubMedDate not supplied

[Lysis of fresh experimental thrombi under the action of a secondary adrenaline-heparin-fibrinogen complex].

It is shown that the epinephrine-heparin-fibrinogen complex, as well as a number of other complex compounds of heparin accomplish the prophylaxis of thrombogenesis at the initial stages of the process, the epinephrine-heparin-fibrinogen complex lysing the thrombi in an average of 48 minutes, while the complexes of fibrinogen-heparin and epinephrine-heparin do this in 2--4 hours. The complex heparin compounds exercise a thrombolytic action only on non-stabilized fresh thrombi with less than 15 minutes from the time of their formation.

Animals↗