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Equilibrium dialysis of metal-serum albumin (Ⅱ)——Allosteric effect in Ni(Ⅱ)-serum albumin systems 总被引:1,自引:0,他引:1
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. 相似文献
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详细研究了Ni~(2+)离子结合于人血清白蛋白(human serum albumin,HSA)和牛血清白蛋白(bovine serum albumin,BSA)的平衡透析.Ni(II)-HSA和 Ni(II)-BSA体系都得到可以划分成两组的8个结合位置,这2个体系都存在2个优先的结合位置,结合于这 2个位置的 Ni~(2+)离子可以看作是别构效应的效应子,诱导的别构效应符合Monod等人建议的模型.别构参数表明,R-态结合Ni~(2+)离子的能力约为T-态的100倍,HSA的构象显著紧于BSA的. 相似文献
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