Zadorozhna M B, Hrynenko T V, Iusova O I, Volkov H L
Ukr Biokhim Zh (1999). 2004 Sep-Oct;76(5):71-7.
Possible interaction of alpha-2-antiplasmin with fibrinogen, fibrin and their fragments independent of factor XIII as well as the inhibitor effect on the Glu-plasminogen activation by tissue activator were studied. It was shown that alpha-2-antiplasmin is adsorbed on desAA- and desAABBfibrin films (Kd 69.0 +/- 1.0 nM 68.6 +/- 5.3 nM, respectively). Glu-Plasminogen has no effect on the inhibitor binding with desAABBfibrin. Alpha-2-antiplasmin shows strong affinity for fibrin D-dimer (Kd 65.0 +/- 4.0 nM) and D-fragment of fibrinogen (Kd 119.0 +/- 21.0 nM), but it does not interact with E-fragment. The inhibitor inside the fibrin clot decreases 10 times the activation rate of Glu-plasminogen by the tissue activator both is the presence and without factor XIII at physiological ratio of Glu-plasminogen, tissue activator, fibrin and alpha-2-antiplasmin. Thus we have shown that fibrinogen/fibrin binds alpha-2-antiplasmin independent of the factor XIII. Binding sites of the inhibitor are localized in D-fragment of fibrinogen and/or fibrin D-dimer. Alpha-2-antiplasmin inhibits the Glu-plasminogen activation by tissue activator on fibrin.
研究了α-2-抗纤溶酶与纤维蛋白原、纤维蛋白及其片段之间可能存在的不依赖于因子XIII的相互作用，以及对组织型纤溶酶原激活剂激活谷氨酸纤溶酶原的抑制作用。结果表明，α-2-抗纤溶酶可吸附在去氨基-和去双氨基-纤维蛋白膜上（解离常数分别为69.0±1.0 nM和68.6±5.3 nM）。谷氨酸纤溶酶原对抑制剂与去双氨基-纤维蛋白的结合没有影响。α-2-抗纤溶酶对纤维蛋白D-二聚体（解离常数65.0±4.0 nM）和纤维蛋白原的D片段（解离常数119.0±21.0 nM）具有很强的亲和力，但不与E片段相互作用。在纤维蛋白凝块内部，无论是在有因子XIII还是无因子XIII的情况下，在谷氨酸纤溶酶原、组织型纤溶酶原激活剂、纤维蛋白和α-2-抗纤溶酶的生理比例下，该抑制剂都会使组织型纤溶酶原激活剂激活谷氨酸纤溶酶原的速率降低10倍。因此，我们已经证明纤维蛋白原/纤维蛋白可独立于因子XIII结合α-2-抗纤溶酶。该抑制剂的结合位点位于纤维蛋白原的D片段和/或纤维蛋白D-二聚体中。α-2-抗纤溶酶可抑制组织型纤溶酶原激活剂在纤维蛋白上激活谷氨酸纤溶酶原。
