Banton C J, Overell B G
Biological Development Unit, Beecham Pharmaceuticals Research Division, Great Burgh, Epsom.
Drugs. 1987;33 Suppl 3:93-6. doi: 10.2165/00003495-198700333-00014.
Use of an immobilised lysine column as a model system to assess the fibrin binding properties of plasminogen and its derivatives showed that anisoylated plasminogen streptokinase activator complex (APSAC) behaved in a manner similar to that of lys-plasminogen, the adsorption being inhibited in the presence of epsilon-aminocaproic acid. In 3 experimental systems using fibrin as the adsorbant, however, APSAC was more firmly bound than plasminogen and was not readily eluted by epsilon-aminocaproic acid.
使用固定化赖氨酸柱作为模型系统来评估纤溶酶原及其衍生物的纤维蛋白结合特性，结果表明，对氨甲酰纤溶酶原链激酶激活剂复合物（APSAC）的行为与赖氨酸-纤溶酶原相似，在ε-氨基己酸存在下吸附受到抑制。然而，在3个以纤维蛋白为吸附剂的实验系统中，APSAC比纤溶酶原结合得更牢固，并且不易被ε-氨基己酸洗脱。
