Andrianov S I, Makogonenko E M, Kudinov S A
Ukr Biokhim Zh (1978). 1992 May-Jun;64(3):14-20.
125I-labeled polymeric fibrin hydrolyzed with plasmin, Val442-plasmin (miniplasmin, Lys530-plasmin (microplasmin) and trypsin has been studied for radioactivity of its separate electrophoretic bands. The reaction of hydrolysis was stopped at a moment of a two-fold decrease of the fibrin clot turbidity (t1/2) at the wave length 350 nm. For plasmin, miniplasmin, microplasmin and trypsin taken in the same caseinolytic activities t1/2 was 12.4, 40.0 164.1 and 76.8 min, respectively. Differences in composition of fibrin digests taken at t1/2, are demonstrated: the content of high-molecular components of digests decreases in the order of plasmin greater than miniplasmin greater than microplasmin greater than trypsin, thus showing differences in the processes of fibrin clot structure disruption by the enzymes.
对用纤溶酶、Val442 - 纤溶酶（微型纤溶酶）、Lys530 - 纤溶酶（微纤溶酶）和胰蛋白酶水解的125I标记的聚合纤维蛋白的各个电泳条带的放射性进行了研究。水解反应在350nm波长下纤维蛋白凝块浊度下降两倍（t1/2）的时刻停止。对于具有相同酪蛋白溶解活性的纤溶酶、微型纤溶酶、微纤溶酶和胰蛋白酶，t1/2分别为12.4、40.0、164.1和76.8分钟。结果表明在t1/2时所取纤维蛋白消化产物的组成存在差异：消化产物中高分子成分的含量按纤溶酶大于微型纤溶酶大于微纤溶酶大于胰蛋白酶的顺序降低，从而表明这些酶在破坏纤维蛋白凝块结构的过程中存在差异。
