Brooks R A, Vymazal J, Goldfarb R B, Bulte J W, Aisen P
Neuroimaging Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892, USA.
Magn Reson Med. 1998 Aug;40(2):227-35. doi: 10.1002/mrm.1910400208.
By combining nuclear magnetic relaxometry on 39 ferritin samples with different iron loading with magnetometry, results were obtained that suggest a new interpretation of the core structure and magnetic properties of ferritin. These studies provide evidence that, contrary to most earlier reports, the ferritin core is antiferromagnetic (AFM) even at body temperature and possesses a superparamagnetic (SPM) moment due to incomplete cancellation of antiparallel sublattices, as predicted by Néel's theory. This moment also provides a likely explanation for the anomalous T2 shortening in ferritin solution. However, the number of SPM moments derived from this model is less than the number of ferritin molecules determined chemically, and a similar discrepancy was found by retrospectively fitting previously published magnetometry data. In other words, only a fraction of the ferritin molecules seem to be SPM. The studies also provide evidence for paramagnetic (PM) Curie-Weiss iron ions at the core surface, where the local Néel temperature is lower; these ions are apparently responsible for the weaker T1 shortening. In fact, the conversion of uncompensated AFM lattice ions to PM ions could explain the small number of SPM particles. The apparent Curie Law behavior of ferritin thus appears to be a coincidental result of different temperature dependences of the PM and SPM components.
通过将对39个具有不同铁负载量的铁蛋白样品的核磁共振弛豫测量法与磁力测量法相结合,获得的结果表明对铁蛋白的核心结构和磁性有了新的解释。这些研究提供了证据,与大多数早期报告相反,即使在体温下铁蛋白核心也是反铁磁性(AFM)的,并且由于反平行亚晶格的不完全抵消而具有超顺磁性(SPM)矩,这是由奈尔理论预测的。这个矩也为铁蛋白溶液中异常的T2缩短提供了一个可能的解释。然而,从这个模型得出的SPM矩的数量少于化学测定的铁蛋白分子的数量,并且通过回顾性拟合先前发表的磁力测量数据也发现了类似的差异。换句话说,似乎只有一部分铁蛋白分子是SPM。这些研究还为核心表面的顺磁性(PM)居里 - 外斯铁离子提供了证据,其局部奈尔温度较低;这些离子显然是较弱的T1缩短的原因。事实上,未补偿的AFM晶格离子向PM离子的转变可以解释少量的SPM颗粒。因此,铁蛋白明显的居里定律行为似乎是PM和SPM成分不同温度依赖性的巧合结果。