Inhibition of non-sulfated and sulfated cationic and anionic trypsins by phage display-selected BPTI variants.

Equilibrium dissociation constants (KD) were determined as described in Experimental Procedures and values were expressed in picomolar units of concentration. Averages ± SEM from two independent KD determinations are indicated. Note that each KD value was determined from five independent binding events (see Figure 4A) and each binding event was assayed in duplicate.

平衡解离常数（Equilibrium dissociation constants, KD）按照实验步骤中描述的方法完成测定，测定结果以浓度单位皮摩尔（picomolar）表示。本文给出了两次独立KD测定的平均值±标准误（Standard Error of the Mean, SEM）。需注意，每个KD值均由五次独立的结合事件测定得到（详见图4A），且每次结合事件均进行了双复孔检测。