Eretskaia E V, Kudinov S A
Ukr Biokhim Zh (1978). 1979 Jul-Aug;51(4):335-9.
Human plasminogen isolated from the placenta serum fraction by means of affinity chromatography was activated by trypsin being in covalent bond with sepharose. The activation is studied as dependent on pH, temperature and the proenzyme-activator ratio in the presence of 25% glycerol as a stabilizing agent and without it. Utilization of the immobilized trypsin as a plasminogen activator makes it possible to transform completely the proenzyme to plasmin varying the plasminogen-trypsin ratio and time of activation when it is conducted under optimal conditions: in the presence of 25% glycerol at pH 7.0-7.1 and the temperature of 30 degrees C.
通过亲和色谱法从胎盘血清组分中分离得到的人纤溶酶原，被与琼脂糖共价结合的胰蛋白酶激活。在存在25%甘油作为稳定剂和不存在甘油的情况下，研究了激活作用对pH、温度和酶原-激活剂比例的依赖性。使用固定化胰蛋白酶作为纤溶酶原激活剂，当在最佳条件下进行激活时，即存在25%甘油、pH为7.0 - 7.1且温度为30℃时，通过改变纤溶酶原-胰蛋白酶比例和激活时间，可以将酶原完全转化为纤溶酶。
