Léger D, Karniguian A, Soria J, Soria C, Legrand Y
Haemostasis. 1985;15(5):293-9. doi: 10.1159/000215162.
The effect of a collagen-derived octapeptide on some properties of thrombin is presented. This peptide provoked a dose- and time-dependent prolongation of the thrombin-induced plasma and fibrinogen clotting time and inhibited the polymerization of fibrin generated from fibrinogen by thrombin. It did not affect the polymerization of fibrin monomers; it was also without effect on the coagulation of plasma or fibrinogen by reptilase. The prolongation of the fibrinogen clotting time depended on the duration of the incubation of thrombin and the octapeptide and not on the duration of the incubation of fibrinogen and the octapeptide. The inhibition was therefore ascribed to an interference with thrombin, rather than with fibrinogen. A preincubation of the octapeptide with thrombin resulted in an inhibition of the thrombin-induced platelet aggregation. The effect of the octapeptide on thrombin has been related to the presence of positively and negatively charged groups, because uncharged analogue sequences were without effect on these activities of thrombin.
本文介绍了一种胶原蛋白衍生的八肽对凝血酶某些特性的影响。该肽可引起凝血酶诱导的血浆和纤维蛋白原凝血时间呈剂量和时间依赖性延长，并抑制凝血酶从纤维蛋白原生成的纤维蛋白的聚合。它不影响纤维蛋白单体的聚合；对蛇毒凝血酶引起的血浆或纤维蛋白原凝固也无影响。纤维蛋白原凝血时间的延长取决于凝血酶与八肽的孵育时间，而非纤维蛋白原与八肽的孵育时间。因此，这种抑制作用归因于对凝血酶的干扰，而非对纤维蛋白原的干扰。八肽与凝血酶预孵育会导致凝血酶诱导的血小板聚集受到抑制。八肽对凝血酶的作用与带正电荷和负电荷基团的存在有关，因为不带电荷的类似物序列对凝血酶的这些活性没有影响。
