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E M Makogonenko

Publications and source records attributed to E M Makogonenko.

31 records · Page 2Linked to original sources
PubMedDate not supplied

[Some properties of Mg 2+, Ca 2+-AtPase of brain microsomal fractions and synaptic plasma membranes in the solubilized state].

Digitonin-solubilized Mg2+, Ca2+-ATPases of the brain microsomal fraction and synaptic plasma membranes are activated against a background of 6.0 mM Mg2+ by 0.001 and 0.03 mM of the added Ca2+ and manifest maximum activity at temperatures or 40-45 and 35-42 degrees C, respectively. The enzymes of the initial membrane preparations are activated by the same concentrations of the added Ca2+ and are characterized by the same temperature dependence. The values of pH-optima of the enzyme activity of both solubilized preparations are 7.0-7.3 and in comparison with pH-dependence of the initial membrane preparations are shifted towards acid side.

Adenosine Triphosphatases↗
PubMedDate not supplied

[The effect of kringles K1-3, K4 and K5 on lysis of fibrin clots caused by the activation of Glu- and Lys-plasminogen by a tissue activator].

Kringles K1-3, K4 and K5 are studied for their effect on tissue plasminogen activator-induced fibrin clot lysis in the presence of Glu- and Lys-plasminogen. It is established that kringles K4 and K5 inhibit fibrinolysis of Glu-plasminogen, and K1-3--that of Lys-plasminogen. The role of plasminogen molecule kringles in the plasminogen interaction with fibrin polymer is discussed.

Blood Coagulation Tests↗
PubMedDate not supplied

[Use of a turbidimetric method to study the kinetics of inhibition of fibrinolysis in diluted blood plasma].

Dependence of fibrinolysis parameters on the concentration of inhibitors of fibrinolytic process has been studied when using turbidimetric method. It is shown that the process of destruction of fibrin clot formed in diluted blood plasma is subjected to the Michaelis-Menten ratio. The constant of inhibition of fibrinolytic process in diluted plasma activated by prothrombin and streptokinase is 10 and 0.5 microM for 6-aminohexanoic acid and contrykal, respectively.

Aminocaproic Acid↗
PubMedDate not supplied

[Fibrin fragment beta 15-118. Inhibitory and complex-forming properties].

Peptide beta 15-118 isolated from desAABB-NDSK preserves fibrin polymerization active site "B", inhibits polymerization process at 12 degrees C, eliminates the inhibitory properties of plasmin D-D-fragment but does not influence inhibitory properties of a D-monomer fragment. Complex formation between peptide beta 15-118 and both D- and D-D fragments was electrophoretically demonstrated. Peptide beta 15-118 forms more stable complex with the D-D fragment which does not dissociate in the medium of polymerizing fibrin as the complex of the peptide with monomer D fragment does. Gel filtration data confirm dimerization of D-monomer fragments after their complexing with beta 15-118. This phenomenon suggests that mutual affinity of D-domains in fibrin increases after loci interactions of the "B"-"b" type.

Antifibrinolytic Agents↗
PubMedDate not supplied

[Study of the polymerization of fibrin using monoclonal antibodies 2D-2A and their Fab-fragments].

It has been shown that monAb's 2d-2a and their Fab-fragments are specific and effective inhibitors of fibrinogen clotting. Only one IgG molecule of monAb's 2d-2a can bind with one of their epitopes situated around peptide bond B beta Arg14-Gly15 in dimer fibrinogen molecule reducing the rate of protofibril lateral association and clot turbidity with only one fibrinopeptide B splitting off per fibrinogen molecule by thrombin. But two molecules of Fab-fragments of monAb's 2d-2a join to both of their epitopes and inhibit fibrinogen clotting dramatically without clot formation and with no fibrinopeptide B splitting off. These data suggest that the site of fibrin protofibril lateral coalescence is localized in NH2-terminal part of fibrin (ogen) B beta-chain, i.e. central E-domain of fibrin molecule takes part in protofibril lateral association. The mutual space orientation of NH2-terminal regions of fibrinogen B beta-chains is discussed.

Antibodies, Monoclonal↗
PubMedDate not supplied

[Heparin effect on hydrolysis of fibrin clots in a bull and a man with varying fibrinolytic systems].

Heparin was studied for its effect on the hydrolysis time of clots from desAA fibrin (FB), desAABB fibrin (F0) and fibrinogen (Fg) of a bull and a man by gly-or lys-plasminogen which is activated by the tissue activator. It is shown that heparin in the concentration to 4.6 M does not affect that hydrolysis time of clots from human and bovine Fg and human Fg by gly-plasminogen which is activated by the tissue activator. Heparin increases the hydrolysis time of clots from bovine Fg and F0 by gly-and lys-plasminogen, the tissue activator being present. It firstly increases (in concentrations below 0.5 (microM), and then decreases (in concentrations above 0.5 (microM) the hydrolysis time of clots from human FB, F0 and Fg and bovine FB and F0 by plasmin. In concentration 4.6 microM heparin increases the hydrolysis time of clots from human fibrinogen by fibrinolytic systems. Effect of heparin on fibrinolytic process from the viewpoint of affine interactions between the components of fibrin clots is discussed.

Animals↗