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57Fe quadrupole splitting and isomer shift in various oxyhemoglobins: study using Mössbauer spectroscopy

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Abstract

A comparative study of normal human, rabbit and pig oxyhemoglobins and oxyhemoglobin from patients with chronic myeloleukemia and multiple myeloma using Mössbauer spectroscopy with a high velocity resolution demonstrated small variations of the 57Fe quadrupole splitting and isomer shift. These variations may be a result of small structural differences in the heme iron stereochemistry of various hemoglobins.

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Authors and Affiliations

  1. Faculty of Physical Techniques and Devices for Quality Control, Ural Federal University (The former Ural State Technical University—UPI), Ekaterinburg, 620002, Russian Federation

    M. I. Oshtrakh & V. A. Semionkin

  2. Hematological Scientific Center of the Russian Academy of Sciences, Moscow, 125167, Russian Federation

    A. L. Berkovsky

  3. Department of Biochemistry, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India

    A. Kumar & S. Kundu

  4. Faculty of Internal Diseases Propedeutics, Ural State Medical Academy, Repin str. 3, Ekaterinburg, 620028, Russian Federation

    A. V. Vinogradov & T. S. Konstantinova

  5. Faculty of Experimental Physics, Ural Federal University (The former Ural State Technical University—UPI), Ekaterinburg, 620002, Russian Federation

    V. A. Semionkin

Authors
  1. M. I. Oshtrakh
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  2. A. L. Berkovsky
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  3. A. Kumar
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  4. S. Kundu
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  5. A. V. Vinogradov
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  6. T. S. Konstantinova
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  7. V. A. Semionkin
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Corresponding authors

Correspondence to M. I. Oshtrakh or S. Kundu.

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Oshtrakh, M.I., Berkovsky, A.L., Kumar, A. et al. 57Fe quadrupole splitting and isomer shift in various oxyhemoglobins: study using Mössbauer spectroscopy. Hyperfine Interact 197, 301–307 (2010). https://doi.org/10.1007/s10751-010-0232-1

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  • DOI: https://doi.org/10.1007/s10751-010-0232-1

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