Equilibrium dialysis of metal-serum albumin (Ⅱ)——Allosteric effect in Ni(Ⅱ)-serum albumin systems

• Published in: Science China. Chemistry Vol. 40; no. 2; pp. 122 - 127
• Main Author: 胡绪英 宋仲容 苏宪东 欧阳砥 黄杰生 周永洽
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer Nature B.V 01.04.1997
• Subjects: albumin; allosteric; Binding sites; constants; Dialysis; effect; equilibrium; Ni{II}-serum; Serum albumin; stability; Stability constants; successive
• ISSN: 1674-7291; 1006-9291; 1869-1870; 1862-2771
• DOI: 10.1007/BF02876402

Detailed studies were carried out on equilibrium dialysis of the binding of Ni2++ ion to human scrum albumin (HSA) and bovine serum albumin (BSA).The successive stability constants were obtained by the Icfisi squares fitting.The eight binding sites found for both Ni(Ⅱ)-HSA and Ni(Ⅱ)-BSA systems can be divided into two different sets; and for both systems,there exist two identical prior binding sites where the bound Ni2+ ions can he con sidered as allosteric effectors,which induce the allosteric effect in accordance with the model proposed by Moeod et al As indicated by allosteric parameters,the ability of R-state to bind Ni2+ ions is ca 100 times as much as that of T state,and the conformation of HSA is markedly tenser than that of BSA.