[Soluble fibrin and D-dimer at normal pregnancy and pregnancy with risk of miscarriage].

ELISA for soluble fibrin (SF) quantification has been elaborated on the basis of our fibrin-specific monoclonal antibodies (mAb). Epitope for these mAb is localized in fibrin fragment Bbeta118-134. The method was used on the blood plasma of healthy pregnant women (control group) and pregnant women with the risk of fetal loss (RFL).

[Quantification of D-dimer and soluble fibrin in blood plasma of people with ischemic heart disease and hypertension].

The method of D-dimer quantification in the human blood plasma has been developed using monoclonal antibodies 111-3b and II-4d. The method has been verified on the blood plasma of the patients with ischemic heart disease with and without stenocardia and with hypertension. The results showed that at ischemic heart disease with and without stenocardia and at hypertension the quantities of D-dimer in the blood plasma were generally less than the highest normal level 500 ng/ml (64.

[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.

[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.

[Study of fibrinogen-fibrin cryocomplexes by a quantitative analysis of N-terminal amino acids].

The reaction between fibrinogen (F) and thrombin (0.003 NIH/ml) has been investigated under physiological conditions. The action of thrombin was inhibited in various time intervals including gel point (4 h), and the reaction mixtures were allowed to stand 0 degrees C.

[Properties of 2 fibrin monomer forms which differ in the degree of thrombin activation. Relation of these 2 forms to specific polymerization inhibitors].

The inhibitory effect of fibrinogen and its fragment D on the clotting of two fibrin monomer species has been studied. One of them (f0) lacks peptides A and B, the other (fB) preserves peptides B. The inhibitors retard the clotting of f0 but fail to influence fB polymerization.

[Properties of 2 fibrin monomer species which differ in the degree of thrombin activation. Characteristics of successively appearing active sites].

Some properties of intermediate and final products of fibrinogen activation by thrombin have been studied. The intermediate (fB) lacks peptide A, the final fibrin (fo)--A and B peptides. Peculiar pH-dependent differences have been observed when examining the effect of ionic strength on polymerization rate of fo and fB.

[Changes in the primary structure of rabbit muscle aldolase under the influence of valine against a background of prolonged fasting].

The primary structure of the muscle aldolase molecule was studied as affected by semilethal doses of valine administered the abdominal cavity of the rabbits after a long fasting. It is established that in spite of differences in the amino acid composition of the protein, uniformity of the peptides distribution in the process of bromo-cyanogen fragments elution and the total amount of amino acid residues in the identical fragments are maintained. Changes are found only in the point-replacements by amino acids in C-fragment of the molecule (asparagine is replaced by valine and threonine by serine).