Sumi H, Takada Y, Takada A
Thromb Haemost. 1978 Feb 28;39(1):46-52.
The esterase activity of highly purified human urokinase on Nalpha-acetylglycl-L-lysine methyl ester is strongly inhibited by 1 X 10(-5) to 1 X 10(-2)M Cu++, Hg++, Ni++, Co++, Fe+++, and Mn++ solutions, whereas Na+, K+, Ca++, and Mg++ are weakly effective. This inhibition is parallel with the inhibition of activation of plasminogenby urokinase. There is no simple linear relation between inhibiton and concentration. Addition of ethylenediaminetetraacetate or electrodialysis fully reactivates the inhibited enzyme. These results are discussed in relation to similar effects of ions on trypsin.
高度纯化的人尿激酶对Nα-乙酰甘氨酰-L-赖氨酸甲酯的酯酶活性,可被1×10⁻⁵至1×10⁻²M的Cu²⁺、Hg²⁺、Ni²⁺、Co²⁺、Fe³⁺和Mn²⁺溶液强烈抑制,而Na⁺、K⁺、Ca²⁺和Mg²⁺的抑制作用较弱。这种抑制作用与尿激酶对纤溶酶原激活的抑制作用平行。抑制作用与浓度之间不存在简单的线性关系。加入乙二胺四乙酸或进行电渗析可使被抑制的酶完全重新激活。结合离子对胰蛋白酶的类似作用对这些结果进行了讨论。