Detailed studies were carried out on equilibrium dialysis of the binding of Ni^(2+)+ion to human scrum albumin(HSA)and bovine serum albumin(BSA).The successive stability constants were obtained by the Icfisi squares f...Detailed studies were carried out on equilibrium dialysis of the binding of Ni^(2+)+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 Ni^(2+)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 Ni^(2+)ions is ca 100 times as much as that of T state,and the conformation of HSA is markedly tenser than that of BSA.展开更多
基金Project supported by the National Natural Science Foundation of China
文摘Detailed studies were carried out on equilibrium dialysis of the binding of Ni^(2+)+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 Ni^(2+)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 Ni^(2+)ions is ca 100 times as much as that of T state,and the conformation of HSA is markedly tenser than that of BSA.
