An increase in the lysis of human and rat clot of euglobulin fraction of blood plasma was caused by an actomyosin preparation isolated from rabbit and rat muscle. Neither fibrinolytic nor activating properties of actomyosin were observed on applying of different concentration (13-0.6 mg/ml) of the protein on the fibrin films. No activation of 0.4% solution of pure plasminogen by actomyosin was observed in vitro. A decrease in fibrin clot density under the effect of actomyosin was indicated by thromboelastogramms of blood plasma and euglobulins. The phenomenon was probably determined by the physicochemical properties of the protein itself.

Actomyosin↗

PubMedDate not supplied

[Fibrinolytic activity of the urine during chronic glomerulonephritis and amyloidosis].

Correlative interconnections between plasminogen activator (PA) activity (fibrin plate method) and level of urokinase antigen (Ag UAP) and tissue PA antigen (Ag TAP) in urine and blood (ELISA) were studied in 60 patients with chronic glomerulonephritis (CGN) and 38 patients with amyloidosis. The high degree of positive correlation between blood and urine initial PA activity and Ag UAP content was found. This suggests the possible leading role of UAP in formation of the basal fluctuations of fibrinolytic activity in blood and urine. High degree of correlation--r = +0.84 and p < 0.001--was found between blood Ag UAP and urine Ag TAP in amyloidosis only. The functional protein loading probe revealed great importance of high urine and blood AP activity in realizing of ultrafiltration renal process--in CGN and amyloidosis.

Amyloidosis↗

PubMedDate not supplied

[Fibrinolysis and the level of fibrin stabilizing factor in patients with cavernous hemangiomas of the maxillofacial region].

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Facial Neoplasms↗

PubMedDate not supplied

[Fractionation of a preparation of fibrinolytic enzymes "tricholysin" formed from Trichotecium roseum Lk. ex Fr. on carboxymethyl-sephadex C-50].

A preparation of fibrinolytic enzymes that produced a specific effect on blood fibrinolysis in animals was isolated from the culture liquid filtrate of the fungus Trichothecium roseum. By gel filtration on KM-Sephadex G-50 six fractions differing in their fibrinolytic, esterase and caseinolytic activities were obtained. The most effective fibrinolytic agents were the first and fourth fractions that had high fibrinolytic and esterase activities and a low caseinolytic activity.

Chromatography, Gel↗

PubMedDate not supplied

[Physico-chemical properties of the thrombolytic compound longolytin].

A preparation exhibiting high fibrinolytic activity and ability to activate plasminogen was isolated from cultivation medium of Arthrobotrys longa. Homogeneous protein, obtained after gel filtration on Sephadex G-100, had molecular mass 28,600, pI-3.68-3.74, optimum activity at pH 6.0-9.0 and temperature optimum at 37 degrees. The enzyme proved to be serine proteinase as shown by analysis using inhibitors; it required thiol groups.

Chromatography, Gel↗

PubMedDate not supplied

[Thrombolytic effect of urokinase upon various methods of administration into the body].

A preparation of urokinase, obtained from human kidney cell culture, was administered into rats at a single dose of 5,000-10,000 U/200 g of body mass in a variety of ways using intravenous, intraperitoneal and subcutaneous inoculations. After intraperitoneal and subcutaneous administrations an increase of fibrinolytic activity in blood was more long-term although less distinct; the phase of reactive hypercoagulation was only slightly detected within 24 hrs after these procedures. Thrombin-produced provocation of thrombosis led to a lesser ratio of death in these animals as compared with the animals group administered intravenously. However, thrombolytic effect of similar doses of urokinase was the highest in intravenous administration. The fibrinolytic activity correlated well with content of the antigen (enzyme) in blood but not with the antiplasmin content in all the procedures used.

Animals↗

PubMedDate not supplied

[Fibrinolytic properties of protease complex isolated from the culture fluid of Nocardia minima].

The protease complex isolated form the Nocardia minima culture liquid was studied in vitro. The preparation had two different activities (fibrinolytic and activating), i.e. it was able to convert plasminogen into plasmin. At a concentration of 250 micrograms/ml and above the preparation lysed experimental thrombi. The fibrinolytic activity of the preparation was completely inhibited with normal human plasma.

Blood Coagulation Tests↗

PubMedDate not supplied

[Study of the thrombolytic and fibrinolytic properties of thiol- dependent serine proteinase (TSP) from Thermoactinomyces vulgaris in vivo].

Experiments on male albino rats showed that the thyol-dependent serine proteinase (TSP) dissolved the thrombus in the jugular vein for 2-5 hr. Intravenous injection of TSP activated the fibrinolytic system of intact animals by increasing the levels of the plasminogen activator and plasmin in the euglobulin fraction. The response of the fibrinolytic system on the intravenous injection of TSP (2mg/200 g) was different: in some rats, fibrinolysis was activated, while on others, it was inhibited. TSP in high doses caused the death of 60% of experimental animals.

Actinomyces↗

PubMedDate not supplied

[Effects of epsilon-aminocaproic acid, amben and kontrikal on fibrinolysis due to tissue-type plasminogen activator from the pig heart].

Simultaneous intravenous administration to rats of epsilon-aminocaproic acid and high doses of plasminogen tissue activator from the pig heart was shown to prevent fibrinolysis changes induced by the tissue activator. Amben completely suppressed the action of the tissue activator at the blood concentration 15 times less than that of epsilon-aminocaproic acid. A greater effect of amben on the blood activator level was noted. Contrykal exerted only slight effect on fibrinolysis stimulated by the tissue activator.

Aminocaproates↗

PubMedDate not supplied

[Effect of synthetic and natural inhibitors on the activity of tissue activator from the swine heart in vitro].

Activity of tissue activator, isolated from pig heart, was studied in vitro in presence of synthetic inhibitors epsilon-aminocapronic acid and amben as well as of natural inhibitor contrical. All the inhibitors studied inhibited the tissue activator as shown by analyses on fibrin plates and by means of quantitative estimation of thrombolytic activity in fibrinolytic preparations in vitro. Among the two synthetic inhibitors amben exhitited the highest effect on the tissue activator: its effect was 3-4-fold higher as compared with epsilon-aminocapronic acid.

Aminocaproic Acid↗

PubMedDate not supplied

[The effect of thymoptin on enzymatic fibrinolysis].

Stimulation of fibrinolysis, decrease in content of fibrinogen and inhibitors were observed after intravenous, intramuscular or subcutaneous administrations of thymoptine preparation (complex of peptides, isolated from mammalian thymus) at doses of 0.1 microgram, 1.0 microgram/200 g of rat body mass. A more long-term effect was found after a course of treatment involving 5 subcutaneous or intramuscular injections (1.0 microgram). Single intravenous administration of thymoptine (0.1 microgram/200 g) caused a moderate thrombolytic action. Development of thrombosis, provoked by subtotal dose of thrombin, was inhibited after subcutaneous injection of the preparation.

Animals↗