Yang H
Abbott Laboratories, Thrombolytics Venture Discovery, Abbott Park, IL 60064.
Thromb Res. 1992 Feb 1;65(3):377-88. doi: 10.1016/0049-3848(92)90168-a.
Effects of water-miscible organic solvents added to an aqueous buffer on the activity of several serine proteinases were studied. Plasmin in particular showed a dramatic difference in activity depending on the hydrophobicity of the added organic solvent through a combination of Km and kcat effects. An inverse linear correlation between the polarity of the mixed solvent and the log (kcat/Km) of plasmin activity was observed for both H-D-Val-Leu-Lys-p-nitroanilide (S-2251) and pro-urokinase as the substrate. The activity of plasmin was less dependent on the polarity of the added solvent when other chromogenic substrates were employed that contained an arginyl residue in the P1 site.
研究了添加到水性缓冲液中的与水混溶的有机溶剂对几种丝氨酸蛋白酶活性的影响。特别是纤溶酶,通过Km和kcat效应的组合,其活性根据添加的有机溶剂的疏水性表现出显著差异。对于作为底物的H-D-缬氨酸-亮氨酸-赖氨酸-对硝基苯胺(S-2251)和尿激酶原,观察到混合溶剂的极性与纤溶酶活性的log(kcat/Km)之间呈反线性相关。当使用在P1位点含有精氨酰残基的其他生色底物时,纤溶酶的活性对添加溶剂的极性依赖性较小。