金属-血清蛋白的结构研究 Ⅲ.Ni^(2+)离子诱导的HSA和BSA的缓慢构象变化(英文)  

Structural Studies on Metal-Serum Albumin III . Slow Conformational Transition of HSA and BSA Induced by Ni^(2+) Ion

作　　者：梁宏[1] 欧阳砥[2] 胡绪英[2] 太俊哲 贺进田[2] 周永洽[2] 

机构地区：[1]广西师范大学化学系,桂林541004 [2]南开大学化学系,天津300071

出　　处：《化学学报》1998年第7期662-667,共6页Acta Chimica Sinica

基　　金：国家自然科学基金(29271025);广西自然科学基金资助课题

摘　　要：用紫外光谱观察到Ni^(2+)离子与人或牛血清白蛋白相互作用有显著的滞后效应,表明Ni^(2+)离子的结合可以诱导入或牛血清白蛋白发生从对Ni^(2+)离子有较弱亲和力至较强亲和力构象态的缓慢变化(T-R转化);这一构象变化为试样的旋光能力随时间变化进一步证实;测得并讨论了这一构象变化的速度常数和活化参数;推测这一构象变化可能主要发生在蛋白质的LA亚区,并且很可能是一种促使IA亚区变得更加开放的“绞链式运动”.A notable hysteretic effect has been observed in the interaction of Ni2+ ion with human or bovine serum albumin using UV - Visible spectrometry, which shows that the binding of Ni2+ ion can induce a slow transition of HSA and BSA from the conformation of weaker affinity for Ni2+ ion to the one of stronger affinity (T - R transition). This conformational transition is supported by the time -dependence of the optical rotation of the samples. The rate constants and activation parameters of these transitions have been measured and discussed. It is inferred that such a conformational transition may mainly occur in the IA subdomain of the proteins,and is likely to be a 'hinged movement', which makes the IA subdomain become more open.

关 键 词：血清白蛋白 滞后效应 构象变化 镍离子 相互作用 

分 类 号：O614.813[理学—无机化学] Q512.102[理学—化学]