Quantitative studies of ferritinlike iron in erythrocytes of thalassemia, sickle-cell anemia, and hemoglobin Hammersmith with Mössbauer spectroscopy.

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Abstract
By using the technique of recoil-free absorption (Mossbauer effect) in Fe, large amounts of Fe were found, yielding a well-defined spectrum different from that of oxy- or deoxyhemoglobin, in whole erythrocytes of 13 patients with .beta.-thalassemia major and intermedia, 3 with Hb H disease, 2 with sickle cell anemia, and 1 with unstable Hb Hammersmith. The Mossbauer spectra at various temperatures of this additional component of Fe were identical to spectra obtained from isolated ferritin or hemosiderin. This observation, together with additional arguments, strongly suggested that the compound responsible for the additional subspectrum was an Fe storage protein, ferritin or hemosiderin. The amounts of ferritin-like Fe were comparable to those of Hb Fe and were particularly large in reticulocytes. No ferritin-like Fe was detected in patients with severe autoimmune hemolytic anemia and pernicious anemia. The large quantities of ferritin-like Fe in hemoglobinopathies were probably due to intracellular Hb denaturation and the consequent release of excess Fe.