Publications by authors named "Kudinov S"

New knowledge concerning the role of inflammation in activation of fibrinolysis and in discoordination of its components interaction has been presented in the review. Considerable attention was given to molecular mechanisms of the haemostatic protein involvement in the acute phase of inflammation. An analysis of their level changes according to inflammation state has been proposed for thrombogenic risk assessment.

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The paper presents the results of a 5-year follow-up of simulative manifestations of tuberculosis at penitentiaries. The high rate of use of penitentiaries as an object of these manifestations has been established, predominantly relapse aggravation of process activity being observed when treatment is continued. The causes of simulative manifestations are diverse; along with a qualitative physical examination, they should be borne in mind by a phthisiatrician in order to make a timely diagnosis.

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Two epidemic outbreaks of tuberculosis were observed among young socially dysadapted individuals at a juvie. They were liquidated, by chiefly implementing social preventive measures and by introducing new chemotherapy regimens.

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The paper is devoted to analysis of the literature data about a recently described component of haemostasis system that posseses carboxypeptidase activity and is activated by thrombin. The history of investigation and isolation of the new carboxypeptidase, their properties and participation in inhibition of fibrinolysis reactions was considered. Data are cited about carboxypeptidase B level changes under different physiological conditions and possible methods of fibrinolysis reactions strengthening by means of influence on activity of that carboxypeptidase.

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The review paper was dedicated to development of the promising photochemical synthesis of affine sorbents for plasminogen isolation from the human blood plasma. Some most interesting, from the viewpoint of practice, types of sorbents and carriers based on high-molecular compounds of natural (organic) or synthetic origin have been considered. The advantages of the use of photochemical synthesis of biospheric sorbent as compared with thermochemical method have been shown.

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Conditions for affine sorbents creation by means of linear photocopolymer photochemical synthesis, its thermochemical granulation-crosslinking, and grafting by L-lysine hydrochloride as an sorbent affinant (ligand) were investigated. Linear photocopolymer properties depending on concentration ratio of photopolymerisation components, chemical nature of reaction media (solvent), and UV irradiation time were studied. Dioxane is shown to be the optimal solvent.

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The thrombolytic treatment with plasminogen activators, such as physiological tissue-type plasminogen activator (t-PA), suffers from a number of significant limitations. There is a resistance to reperfusion and acute coronary reocclusion. The peculiarity of t-PA and one-chain urokinase treatment is their using in very high doses.

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A single factor V gene G-A mutation (Arg506Gln) underlying activated protein C (APC) resistance is a common risk factor for venous thromboembolism. It is still unclear whether the factor V Leiden predisposes patients to arterial thrombosis and myocardial infarction (MI). To determine a correlation between the factor V Leiden mutation and MI in different age categories, DNA samples from 287 patients with "early" and "late" MI were investigated.

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Plasminolysis of the fibrinogen arginine and its DH-fragment residues was sufficiently lower in contrast to that of initial proteins. It is supposed that the decrease of the speed of the process is the result of the blocking of centres, adequate to arginyl-binding sites of plasmin molecule.

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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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A scheme of in vitro formation and hydrolysis of the fibrin clot is suggested. This scheme considers the data concerning a cofactor role of fibrin in activation of polymerization and fibrinolysis. Such parameters of a number of components as concentration of A-, B beta 1-42-and B beta 15-42 peptides and of other fragments of fibrinogen which allow characterizing a state of hyperfibrinolysis, hyperclotting or dynamic equilibrium of these systems are selected in the scheme.

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125I-labeled polymeric fibrin hydrolyzed with plasmin, Val442-plasmin (miniplasmin, Lys530-plasmin (microplasmin) and trypsin has been studied for radioactivity of its separate electrophoretic bands. The reaction of hydrolysis was stopped at a moment of a two-fold decrease of the fibrin clot turbidity (t1/2) at the wave length 350 nm. For plasmin, miniplasmin, microplasmin and trypsin taken in the same caseinolytic activities t1/2 was 12.

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Glu- and Lys-plasminogen interaction with native and desAABB-fibrin obtained from fibrinogen partially hydrolyzed by plasmin was studied. It was found that native fibrin adsorbs 6 times more Lys-plasminogen as compared to the native form of the proenzyme. The range of the Lys-plasminogen binding does not change, if part of the fibrinogen molecules hydrolyze down to X-fragments.

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A diagnostic method is described for determining the parameters of the human blood plasma coagulation and fibrinolysis by turbidimetry. Diluted plasma with thrombin and streptokinase is mixed to initiate clot formation and subsequent clot dissolution. The resultant profile of absorbance versus time is analysed to determine six parameters: plasma coagulation time, the rate of coagulation, fibrinogen concentration, the rate of fibrinolysis, fibrin clot half-lysis and lysis time.

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A comparative analysis of the rates of polymeric fibrin structure destruction by plasmin (Pm) and its proteolytic derivatives such as Val354-plasmin (c-Pm), Val442-plasmin (m-Pm) and Lys530-plasmin (mu-Pm) has been undertaken. It was shown, that Pm, c-Pm, m-Pm and mu-Pm at equal proteolytic activity, have dissolved fibrin clots with relative rates 40.3:38.

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The rate of plasmin or Val442-plasmin catalyzed hydrolysis of fibrinogen decreases several times as affected by arginine in high concentrations. The enzyme is shown to be not inhibited by arginine. The observed effect is supposed to depend on saturation of the protein-proteins interaction sites located between 442 and 790 amino acid residues.

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Fibrinogen-NDSK complex is a model of protofibril having some features of the fibrin polymer structure. This complex has been studied for its ability to stimulate the plasminogen activation by t-PA. The fibrinogen-NDSK complex have increased the rate of plasminogen activation by t-PA as compared to fibrinogen or NDSK taken separately.

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Glu-plasminogen interaction with fibrinogen fragment E results in the alteration of its adsorptive capacity. During this interaction in the absence of plasmin and tissue activator of plasminogen, Glu-plasminogen is transformed into a partly degraded form. Glu-plasminogen complexes with soluble and immobilized fibrinogen fragment E.

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The ligand binding of kringle 1 + 2 + 3 and kringle 1 from human plasminogen has been investigated by fluorescence spectroscopy. Analysis of fluorescence titration of kringle 1 + 2 + 3 with 6-aminohexanoic acid shows that this fragment, besides the high-affinity lysine-binding site with Kd = 2.9 microM, contains two additional lysine-binding sites which differ in binding strength (Kd = 28 microM and Kd = 220 microM).

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Affinity of plasminogen fragments K1, K2-3, K4 and K5 for 6-aminophenyl-Sepharose was investigated to characterize the lysine-binding sites of the protein. K1 and K5 fragments were bound to the affinity column, whereas kringle 2-3 and kringle 4 were not. The results obtained and data known from literature have indicate that two types of lysine-binding sites are present in the plasminogen molecule.

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The effect of heparin on the proteolytic and fibrinolytic activities of plasmin and plasminogen was studied. Heparin at a concentration of 6.3.

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Trypsin from pyloric caeca of Pacific salmon was purified by affinity chromatography of the water extract on hexamethylenediamine-glycidylmethacrylate-cellulose. A protein band with a molecular weight of 22.5 kDa was found on SDS-electrophoresis in PAG.

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The ability of the native form of plasminogen (Glu-plasminogen) to form complexes with fibrinogen and its fragments immobilized on CNBr-agarose was studied. It was found that unlike Lys-plasminogen, the native form of the proenzyme does not bind to fibrinogen agarose. Limited proteolysis of fibrinogen by plasmin involving alpha C-domains results in the appearance of Glu-plasminogen binding sites at fibrinogen surface.

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