Ts'ao C, Galluzzo T S
Am J Clin Pathol. 1981 Mar;75(3):372-7. doi: 10.1093/ajcp/75.3.372.
The ability of human plasma and purified human plasmin and plasminogen to hydrolyze a new synthetic substrate, H-D-valine-leucine-lysine-5-aminoisophthalic acid, dimethyl ester, ditrifluoroacetate, was studied. Contrary to published data, we found this substrate was only minimally hydrolyzed by plasmin or urokinase-treated plasminogen or plasma. Plasminogen-free bovine fibrinogen was readily degraded by plasmin and urokinase-activated plasminogen. However, in the presence of streptokinase, the synthetic substrate was highly sensitive to human plasma and purified plasmin and plasminogen. Apparently, the substrate is specific for streptokinase-plasmin and streptokinase-plasminogen activators, not for plasmin.
研究了人血浆、纯化的人纤溶酶和纤溶酶原水解一种新的合成底物H-D-缬氨酸-亮氨酸-赖氨酸-5-氨基间苯二甲酸二甲酯、二氟乙酸盐的能力。与已发表的数据相反，我们发现该底物仅被纤溶酶、尿激酶处理的纤溶酶原或血浆轻微水解。无纤溶酶原的牛纤维蛋白原很容易被纤溶酶和尿激酶激活的纤溶酶原降解。然而，在链激酶存在的情况下，该合成底物对人血浆、纯化的纤溶酶和纤溶酶原高度敏感。显然，该底物对链激酶-纤溶酶和链激酶-纤溶酶原激活剂具有特异性，而对纤溶酶没有特异性。
