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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1979 Feb;76(2):939–943. doi: 10.1073/pnas.76.2.939

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

E R Bauminger, S G Cohen, S Ofer, E A Rachmilewitz
PMCID: PMC383099  PMID: 284419

Abstract

By using the technique of recoil-free absorption (Mössbauer effect) in iron, we found large amounts of iron, 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 hemoglobin H disease, 2 with sickle-cell anemia, and 1 with unstable hemoglobin Hammersmith. The Mössbauer spectra at various temperatures of this additional component of iron were found to be identical to spectra obtained from isolated ferritin or hemosiderin. This observation, together with additional arguments, strongly suggests that the compound responsible for the additional subspectrum is an iron storage protein, ferritin or hemosiderin. The amounts of ferritinlike iron were comparable to those of hemoglobin iron and were particularly large in reticulocytes. No ferritinlike iron was detected in patients with severe autoimmune hemolytic anemia and pernicious anemia. The large quantities of ferritinlike iron in hemoglobinopathies are probably due to intracellular hemoglobin denaturation and the consequent release of excess iron.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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