Biopolymers and cell. 1996; 12 (6): 94 - 101

The influence of 6AHA and a2-antip\asm\n on the fibrinolysis in normal, Pg-deficient and (Pg-ta2-antiplasmin)-deficient plasmas studied by turbidimetric method

A. E. Gutsalo

It has been shown that in normal plasma both 6AHA and a2-AP binds only with one site ofPg activated by strepok.in.ase. At has been demonstrated however that 6 AH A (in micromotor concentrations) and a2-AP effects on the different stages of fibrinolysis: 6AHA prevents the binding of Pg to fibrin (first stage of fibrinolysis), while a2-AP does not influence on this stage but delays the accelerated (second) stage of fibrinolysis. The mechanism of such action is discussed. At has been also stated that 6AHA posseses no inhibitory effect on a2-AP during fibrinolysis in plasma. On the contrary to the pure system 6 AH A poten¬tiated the inhibitory influence ofa2-AP on the fibrinolysis in plasma in micromolar concentrations. When the action of 6 AH A on the Pg-deficient and (Pg + a2-AP)~deficient plasma was studied, it has been show that the dependence of clot half lysis from concentration of 6 AH A has parabolic character as opposed to normal plasma where it has linear character. The mechanism of such action is hypothesized.