Abstract
Ferritin, the iron-storing protein of mammals, is known to darken T(2)-weighted MR images. This darkening could be used for the non-invasive measurement of an organ's iron content. Unexplained discrepancies exist between T(2) data obtained in ferritin-containing tissues and aqueous solutions of ferritin. The clustering of the protein induced by trypsin is used to evaluate the effect of ferritin agglomeration on the relaxation rates. Although the longitudinal relaxation is not significantly influenced by clustering, T(2) depends greatly on the stage of agglomeration: the transverse relaxation rate is higher for a clustered sample than for an unclustered sample. Moreover, the field and inter-echo time dependences of the relaxation rate indicate that the relaxation mechanism may be different between small clusters -- where a linear dependence of 1/T(2) on B(0) is observed -- and large clusters -- where a quadratic dependence is observed. These results help to explain the relaxation induced by ferritin in tissues.
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