Halvorsen S, Skjønsberg O H, Godal H C
Department of Internal Medicine, Ullevaal Hospital, Oslo, Norway.
Blood Coagul Fibrinolysis. 1993 Feb;4(1):133-7.
High molecular weight, low molecular weight and very low molecular weight fibrinogen were purified from human plasma, and converted partially or completely to fibrin by the action of thrombin or batroxobin. The stimulatory effects of these fibrin(ogen) preparations on plasminogen activation by tissue plasminogen activator were studied. When only 3-30% of the fibrinogen molecules were converted to fibrin, the high molecular weight fibrin had a greater stimulatory effect on plasminogen activation than equal amounts of low and very low molecular weight fibrin. In completely converted fibrin preparations, the plasminogen activating capacity of high molecular weight fibrin was either equal to (thrombin treated preparations) or greater than (batroxobin-treated preparations) that of very low molecular weight fibrin. These findings suggest that degradation of the A alpha-chain of fibrin does not per se increase its plasminogen activating capacity.
从人血浆中纯化出高分子量、低分子量和极低分子量的纤维蛋白原,并通过凝血酶或巴曲酶的作用将其部分或完全转化为纤维蛋白。研究了这些纤维蛋白(原)制剂对组织型纤溶酶原激活物激活纤溶酶原的刺激作用。当仅3%-30%的纤维蛋白原分子转化为纤维蛋白时,高分子量纤维蛋白对纤溶酶原激活的刺激作用大于等量的低分子量和极低分子量纤维蛋白。在完全转化的纤维蛋白制剂中,高分子量纤维蛋白的纤溶酶原激活能力与极低分子量纤维蛋白的纤溶酶原激活能力相等(凝血酶处理的制剂)或更强(巴曲酶处理的制剂)。这些发现表明,纤维蛋白Aα链的降解本身不会增加其纤溶酶原激活能力。