[Effect of chemical modification of arginine residues of fibrinogen and its DH-fragment on the rate of hydrolysis of these proteins by plasminogen].

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.

[Features of the interaction of Glu- and Lys-forms of plasminogen with native and partially hydrolyzed fibrin].

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.

[The effect of arginine on hydrolysis of fibrinogen by plasmin and mini-plasmin].

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.

[Proteolytic activity of the Glu-plasminogen complex with fibrinogen fragment E].

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.

[Binding of Glu-plasminogen by fibrinogen and byproducts of its proteolysis].

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.