Williams J, Chasteen N D, Moreton K
Biochem J. 1982 Mar 1;201(3):527-32. doi: 10.1042/bj2010527.
The salt dependence of the iron-binding properties of transferrin was studied by urea/polyacrylamide-gel electrophoresis. The distribution of iron between the N-terminal and C-terminal binding sites under equilibrium conditions and the rates of release of iron from the two sites were studied. It was found that salt increases the thermodynamic stability of iron binding in the N-terminal site relative to the C-terminal site. Similar behaviour is observed for the kinetics of iron release, where salt retards the rate of removal of iron from the N-terminal site but facilitates removal from the C-terminal site.
通过尿素/聚丙烯酰胺凝胶电泳研究了转铁蛋白铁结合特性的盐依赖性。研究了平衡条件下铁在N端和C端结合位点之间的分布以及铁从这两个位点释放的速率。结果发现，相对于C端位点，盐增加了N端位点中铁结合的热力学稳定性。在铁释放动力学方面也观察到类似的行为，即盐会减缓铁从N端位点的去除速率，但促进铁从C端位点的去除。
