The 57 Fe hyperfine interactions in iron storage proteins in liver and spleen tissues from normal human and two patients
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The 57 Fe hyperfine interactions in iron storage proteins in liver and spleen tissues from normal human and two patients with mantle cell lymphoma and acute myeloid leukemia: a M¨ossbauer effect study M. I. Oshtrakh · I. V. Alenkina · A. V. Vinogradov · T. S. Konstantinova · V. A. Semionkin
© Springer International Publishing Switzerland 2014
Abstract Study of human spleen and liver tissues from healthy persons and two patients with mantle cell lymphoma and acute myeloid leukemia was carried out using M¨ossbauer spectroscopy with a high velocity resolution. Small variations in the 57 Fe hyperfine parameters for normal and patient’s tissues were detected and related to small variations in the 57 Fe local microenvironment in ferrihydrite cores. The differences in the relative parts of more crystalline and more amorphous core regions were also supposed for iron storage proteins in normal and patients’ spleen and liver tissues. Keywords M¨ossbauer spectroscopy · Hyperfine interactions · Liver and spleen tissues · Ferritin · Iron core · Hematological malignancies
1 Introduction Liver and spleen tissues contain a large amount of iron deposited in iron storage proteins ferritin and hemosiderin. Ferritin consists of a nanosized ferrihydrite (5Fe2 O3 ×9H2 O) iron core, which contains some inorganic phosphates, surrounded with 24 protein subunits shell
Proceedings of the 5th Joint International Conference on Hyperfine Interactions and International Symposium on Nuclear Quadrupole Interactions (HFI/NQI 2014) Canberra, Australia, 21–26 September 2014 M. I. Oshtrakh () · I. V. Alenkina · V. A. Semionkin Department of Physical Techniques and Devices for Quality Control, Institute of Physics and Technology, Ural Federal University, Ekaterinburg, 620002, Russian Federation e-mail: [email protected] M. I. Oshtrakh · I. V. Alenkina · V. A. Semionkin Department of Experimental Physics, Institute of Physics and Technology, Ural Federal University, Ekaterinburg, 620002, Russian Federation A. V. Vinogradov · T. S. Konstantinova Ural State Medical University, Repin str., 3, Ekaterinburg, 620028, Russian Federation
M. I. Oshtrakh et al.
[1]. The cavity for the iron core is about 8 nm and the largest amount of iron atoms may be of about 4500. Hemosiderin is considered as denatured ferritin. In the case of pathologies related to the iron status disorder in the body the iron core structure and size may vary from more amorphous to more crystalline and from smaller to larger size. Ferritin, hemosiderin and tissues containing these biomolecules have been intensively studied using M¨ossbauer spectroscopy for a long time (for review see [2, 3] and references therein). These results demonstrated that variations in the iron core structure may be reflected by the 57 Fe hyperfine parameters. Recent applications of M¨ossbauer spectroscopy with a high velocity resolution demonstrated possibilities to reveal new more precise information in biomedical research due to much better fitting of complicated M¨ossbauer spectra and distinguishing of sma
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