[Effect of low-molecular peptides on the transformation of fibrinogen into fibrin].

The influence of synthetic peptides on fibrinogen transformation to fibrin under the action of thrombin and fibrin-monomer polymerization was investigated. Peptides Gly-Pro-Arg-Pro; Gly-Pro-Arg-Pro-Lys; Gly-Pro-Arg-Pro-Lys-Boc; Gly-Pro-Arg-Pro-Arg are specific inhibitors of fibrin formation. These peptides interfere with the hydrolysing effect of thrombin due to binding to the central domain of fibrinogen.

[Effect of the antioxidant OP-6 on some model reactions of the blood coagulation system].

Formation and lysis of fibrin clot were studied in model systems containing antioxidant OP-6, which is concerned with substances of 3-hydroxypyridine class, using viscosimetry, UV- and IR-spectroscopy. The antioxidant was shown to react with fibrin-monomer molecules shifting an equilibrium of the monomer/polymer/aggregate system towards monomer. OP-6 was able to bind heparin reversibly with formation of the dissociation complex.

Mechanism of the action of factor XIII on the structure of fibrin in the normal and pathological states.

The work discusses the influence of factor XIII on the molecular structure of fibrin and its properties under normal conditions and in certain forms of coagulopathies. It was shown that the reaction of stabilization is accompanied by an exothermic effect, the thermal effect of which on donor blood plasma is 15.5 kcal/mole.