本文選題：頭孢尼西鈉 + 熒光��； 參考：《安徽醫(yī)科大學(xué)學(xué)報(bào)》2017年01期

【摘要】：目的運(yùn)用熒光和紫外光譜法,在不同的溫度下去探討頭孢尼西鈉(CS)與牛血清白蛋白(BSA)的相互作用。方法用Stern-Volmer、Lineweaver-Burk和雙對(duì)數(shù)方程計(jì)算了速率常數(shù)(K_q)、猝滅常數(shù)(K_(sv))、靜態(tài)熒光猝滅締合常數(shù)(K_(LB))、結(jié)合位點(diǎn)數(shù)(n)和有效結(jié)合常數(shù)(K_b)。結(jié)果 CS能結(jié)合BSA。由于生成CS-BSA復(fù)合物,頭孢尼西鈉對(duì)BSA的猝滅是靜態(tài)猝滅機(jī)制。熱力學(xué)參數(shù)表明是一個(gè)自發(fā)過(guò)程,其作用力類型主要為靜電作用力。BSA的亞螺旋域ⅡA是主要結(jié)合位置,離酪氨酸殘基更近。有藥物負(fù)協(xié)同作用。同步熒光光譜法表明CS能改變BSA的色氨酸和酪氨酸殘基的微環(huán)境。結(jié)論 CS與BSA發(fā)生了靜態(tài)相互作用,有一個(gè)結(jié)合位點(diǎn),為CS的臨床研究提供重要的參考依據(jù)。
[Abstract]:Objective to investigate the interaction between cefonesian sodium (CSA) and bovine serum albumin (BSA) at different temperatures by fluorescence and UV spectroscopy. Methods by using Stern-Volmerer Lineweaver-Burk and double logarithmic equations, the rate constant KQ, the quenching constant, the static fluorescence quenching association constant and the binding site number of K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S, K / S and K / S / Results CS could bind to BSA. Because of the formation of CS-BSA complex, the quenching of BSA by cefnesian sodium is a static quenching mechanism. The thermodynamic parameters show that it is a spontaneous process, and the type of force is mainly electrostatic force. The subhelical domain 鈪，

本文編號(hào)：1845379