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Biomedical subjects

L D Azieva

Publications and source records attributed to L D Azieva.

13 recordsLinked to original sources
PubMed1986

[Hemostatic system function as affected by thromboplastic agents from higher plants].

It has been determined that the thromboplastic agents from the inflorescence of the birch Betula pendula Roth, blossoms of the willow Salix daphnoides Vill., seeds of the pea Pisum sativum L. provoke protective reaction of the animal's anticoagulation system, though weaker expressed than the reaction of thromboplastin from brain. The mechanisms of action of thromboplastic agents of plant origin is similar to the mechanism of action of tissue thromboplastin.

Animals↗
PubMed1985

[Mechanism of inhibition of non-enzymatic fibrinolysis by a spleen factor].

Some data on the mechanism of inhibition of non-enzymatic fibrinolysis by a spleen factor are presented. It is demonstrated that the spleen protein factor which interacts with heparin at certain ratios forms a complex with the latter. As a result, the anticoagulating activity and properties of the spleen factor as a non-enzymatic fibrinolysis inhibitor are blocked.

Animals↗
PubMedDate not supplied

[A comparative study of the action of preparations of high- and low-molecular weight heparin on hemostatic indices in vitro and in their intravenous administration to animals].

Low-molecular heparin preparations (a Soviet sample and that manufactured by the Celsus Company) in vitro, added to bovine plasma possess a lower antifactor-II activity, less time of recalcification and partial thromboplastin time as compared to high-molecular heparin of equal concentration (mg/ml) or dose (Units/ml). After intravenous injection of low-molecular heparin preparations to animals in a dose of 50 Units/200 g bw the time of hemorrhage was far less, while anticoagulant activity was lower than in animals given the same dose of high-molecular heparin. Both injection of low-molecular and high-molecular heparin results in a rise of the intensity of non-enzymatic fibrinolysis in the animals' blood plasma.

Animals↗
PubMedDate not supplied

[Heparin from the meadowsweet (Filipendula ulmaria) and its properties].

In the present work, the nature of an anticoagulant from Philipendula ulmaria was studied. A method for purification of this anticoagulant was developed. Using diverse methods it was shown that the molecular weight, data on element (sulphur, nitrogen, and hydrogen) content, spectral characteristics in the infrared region of the spectrum, and electrophoretic properties of the product indicate its similarity to heparin of animal origin.

Animals↗
PubMedDate not supplied

[The effect of tuftsin on fibrin polymerization in vitro and on the hemostatic system when administered intravenously to healthy animals].

Taftsine tetrapeptide has antiprocoagulatory properties in vitro in the presence of plasma. Taftsine exerts depolymerization influence on fibrin monomer in concentrations of 10(-1) to 10(-9) mg/ml. At intravenous injection in doses of 1 mg and 300 ug/kg, taftsine causes the increase in plasma clotting time and significant increase in enzymatic and nonenzymatic fibrinolysis. The effect can be observed during 120 min after injection of the peptide.

Animals↗
PubMedDate not supplied

[Complex compounds of heparin with blood proteins and their natural inhibitors in splenectomy in animals].

In depression of the function of the anticoagulating system after splenectomy in rats the blood serum heparin level diminishes, the fibrinogen concentration increases, the total and nonenzymatic fibrinolytic activity decreases, and the activity of some heparin complexes (adrenaline-heparin and serotonin-heparin) increases. A low-molecular protein inhibiting nonenzymatic fibrinolytic activity was isolated from blood plasma of splenectomized animals, some of its properties were studied. No such protein inhibitor was found in blood plasma of false-operated and intact rats.

Animals↗
PubMedDate not supplied

[The content of a heparin-like anticoagulant in the flowers of the meadowsweet (Filipendula ulmaria)].

The flowers of Filipendula ulmaria were found to contain heparin bound to the plant proteins in the form of a complex. This complex enhances the anticoagulant and fibrinolytic properties of the nonenzymatic nature at its administration to animals both intramuscularly and intravenously. The neutralizing effect of protaminesulphate on the anticoagulant activity of the plant heparin was shown. The identity of the action on the hemostasis system of heparin of animal and plant origin was found.

Animals↗
PubMedDate not supplied

[Heparin-histamine complex, its physico-chemical and biological properties].

Complexes between heparin and histamine at various ratio exhibited various physiological activity. The complex containing heparin-histamine at the ratio of 6:1, 10:1 or 15:1 showed anticoagulation, antipolymerization and nonenzymatic fibrinolytic effects. The complex dissociated in circulation within 90 min after its administration. This complex effected also the rheologic properties of blood.

Animals↗
PubMedDate not supplied

[Cationic proteins from neutrophils as inhibitors of nonenzymatic fibrinolytic and anticoagulant activity of blood plasma].

Two cation proteins free of enzymatic activity, containing one and four peptides (CP-1 and CP-4, respectively), were studied. The cation protein consisting of four peptides proved to be the most effective inhibitor of the nonenzymatic fibrinolytic activity of heparin-containing complexes. Both these cation proteins inhibited similarly the anticoagulation activity of blood plasma. The drugs, like cation proteins, appear to be potentially important for clinical practice under conditions of excessive hemorrhage caused by elevated level in circulation of complexes containing heparin and proteins.

Animals↗
PubMedDate not supplied

[Isolation and various physico-chemical properties of diabetogenic factor from the blood of patients with diabetes].

A preparation of diabetogenic factor was purified 660-fold using affinity chromatography on heparin-Sepharose. Homogeneity of the preparation and its molecular mass (about 60 kDa) were evaluated in, polyacrylamide gel electrophoresis. The fraction with high affinity to heparin exhibited the highest biological activity and was eluted by a solution with high ionic strength (1.5 M NaCl). Biological activity of the diabetogenic factor preparation correlated with its concentration in blood plasma in vitro.

Chromatography, Affinity↗
PubMedDate not supplied

[Characteristics of a heparin-inhibiting spleen protein factor].

A low molecular protein with molecular mass about 15 kDa was isolated from spleen of healthy rabbits and rats. Spectral, electrophoretic properties and amino acid composition of the protein were studied. Biological activity of the protein was connected with inhibitors of nonenzymatic fibrinolysis.

Amino Acids↗