Calisch M P, Topham R W
Int J Biochem. 1984;16(11):1127-34. doi: 10.1016/0020-711x(84)90005-3.
The inhibitor of the serum ferroxidases, recently detected in rabbit serum, has been purified to homogeneity from human serum by a combination of gel-filtration and ion-exchange chromatography. The molecular weight, chromatographic behavior, electrophoretic mobility, electrofocusing pH, carbohydrate content, and reactivity with anti-human albumin during immunodiffusion indicate that the ferroxidase inhibitor is serum albumin. Copper-binding studies, proteolytic fragmentation studies, and a comparison of the inhibitory potencies of several albumin species which differ in their affinity for copper strongly indicate that albumin elicits its inhibitory effect on the serum ferroxidases by interacting with the functional copper of these enzymes. Kinetic analyses further suggest that albumin competes with substrate (ferrous iron) for binding to the functional copper of the serum ferroxidases.
最近在兔血清中检测到的血清铁氧化酶抑制剂，已通过凝胶过滤和离子交换色谱相结合的方法从人血清中纯化至同质。分子量、色谱行为、电泳迁移率、等电聚焦pH值、碳水化合物含量以及免疫扩散过程中与抗人白蛋白的反应性表明，铁氧化酶抑制剂是血清白蛋白。铜结合研究、蛋白水解片段化研究以及对几种对铜亲和力不同的白蛋白种类的抑制效力比较有力地表明，白蛋白通过与这些酶的功能性铜相互作用而对血清铁氧化酶产生抑制作用。动力学分析进一步表明，白蛋白与底物（亚铁离子）竞争结合血清铁氧化酶的功能性铜。
