盐酸异丙肾上腺素与牛血清白蛋白相互作用

摘要

Mechanism of interaction between bovine serum albumin (BSA)and isoprenaline hydrochloride (IH) was studied by fluorospectrometry and capillary zone electrophoresis. As shown by the results of fluorospectrometry, significant quenching of fluorescence of BSA was found by its reaction with IH, and as judging from the fluorescene quenching constants (Kq = 2. 53 × 1013 L · mol-1 · s-1) obtained by Stern-Volmer equation, fluorescence quenching of BSA by IH was attributed to static quenching. The binding constant and number of binding site were found to be 1. 72×101 L · mol-1 and 1 by applying the equation of site-binding mode respectively. It was shown by the results of capillary zone electrophoresis that: values of binding constant and number of binding site were found to be 4. 07 × 101L · mol-1 and 1 respectively.%采用荧光猝灭法和毛细管区带电泳法研究了盐酸异丙肾上腺素(IH)与牛血清白蛋白(BSA)的相互作用.荧光猝灭法研究表明:IH对BSA有较强的荧光猝灭作用,根据Stern-Volmer方程得到猝灭速率常数(Kq)为2.53×1013L·mol-1·s-1,该荧光猝灭属于静态猝灭.采用位点结合模型公式计算得结合常数为1.72×104L·mol-1,结合位点数n为1;毛细管区带电泳法研究表明:IH与BSA的结合常数为4.07×104L·mol-1,结合位点数n为1.