[Fibrinolysis in vitro by acylated derivatives of a plasmin-streptokinase activator complex].
Three active-site-acylated derivatives of the activator plasmin-streptokinase complex have been synthesized: n-anisoyl-, n-trans-(N,N,N-trimethylamino)-cinnamoyl- and n-guanidine-benzoyl-plasmin-streptokinase. Their diacylation rate constants were 4.2 x 10(-4), 2.0 x 10(-4) and 0.6 x 10(-4) s-1, respectively. Kinetics of lysis of fibrin clots, containing plasminogen or plasminogen and alpha 2-antiplasmin, by acylplasmin, by a free activator complex and by two acylated activator complexes has been studied. It is shown that in the presence of zymogen and inhibitor the effect of acylactivator, as a fibrinolytic, is 163 times more effective than that of acylenzyme and the fibrinolytic response increases with the doze of acylactivator. The rate of fibrinolysis by a free plasmin-streptokinase complex was higher without the inhibitor than that of fibrinolysis by its acylated derivatives; fibrinolytic action of acylactivators was more effective in the presence of the inhibitor.
Aĭsina
R B
RB
Popova
G Iu
GIu
Eremeev
N L
NL
Kazanskaia
N F
NF
D000215:Acylation; D016255:Anistreplase / Q000378:metabolism*; D000933:Antifibrinolytic Agents / Q000378:metabolism; D001665:Binding Sites; D005342:Fibrinolysis; D006801:Humans; D007700:Kinetics; D010958:Plasminogen / Q000378:metabolism
D000933:Antifibrinolytic Agents; D016255:Anistreplase; D010958:Plasminogen
Fibrinoliz in vitro atsilirovannymi proizvodnymi aktivatornogo kompleksa plazmin-streptokinaza.