Hyperfine interactions in the iron cores from various pharmaceutically important iron-dextran complexes and human ferritin: A comparative study by Mössbauer spectroscopy / Oshtrakh M.I., Semionkin V.A., Prokopenko P.G., Milder O.B., Livshits A.B., Kozlov A.A. // International Journal of Biological Macromolecules. - 2001. - V. 29, l. 4-5. - P. 303-314.

ISSN:
01418130
Type:
Article
Abstract:
Mössbauer spectroscopy has been used to study the hyperfine interactions in the iron cores of pharmaceutically important industrial and elaborated iron-dextran complexes (ferritin models) and human ferritin. Mössbauer spectra of frozen solutions and lyophilized samples of iron-dextran complexes at 87 K demonstrated magnetic, superparamagnetic and paramagnetic states of iron in various complexes. Mössbauer spectra of human ferritin in frozen solution and lyophilized form showed paramagnetic state of iron at 87 K. Small variations of Mössbauer hyperfine parameters were observed for different samples at 87 and 295 K, respectively, supposing the homogenous iron cores. The values of quadrupole splitting for iron-dextran complexes and ferritin in frozen solutions at 87 K varied from 0.639 to 0.744 mm/s while those of lyophilized samples at 87 K varied from 0.714 to 0.788 mm/s. The values of quadrupole splitting for iron-dextran complexes and ferritin in lyophilized form at 295 K varied from 0.687 to 0.741 mm/s. The values of hyperfine magnetic fields on the 57Fe nuclei in several iron-dextran complexes at 87 K varied from ∼231 to ∼485 kOe. These small variations of the hyperfine parameters were related to several types of the hydrous iron oxide microstructural modifications in the core and variations of the iron core size. The influence of lyophilization on the iron core structure was also assumed. In addition, Mössbauer spectra were evaluated in supposition of heterogeneous iron core in all samples. Copyright © 2001 Elsevier Science B.V.
Author keywords:
Ferritin; Hyperfine interactions; Iron core; Iron-dextran complexes; Mössbauer spectroscopy
Index keywords:
ferritin; iron dextran; article; drug structure; Mossbauer spectroscopy; Dextrans; Ferric Compounds; Ferritins; Humans; Iron; Protein Binding; Spectroscopy, Mossbauer; Stereoisomerism; Temperature; Th
DOI:
10.1016/S0141-8130(01)00181-7
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Affiliations Division of Applied Biophysics, Faculty of Physical Techniques and Devices for Quality Control, Ural State Technical University, Ekaterinburg 620002, Russian Federation; Faculty of Experimental Physics, Ural State Technical University, Ekaterinburg 620002, Russian Federation; Faculty of Biochemistry, Russian State Medical University, Moscow, Russian Federation; Hematological Scientific Center, Russian Academy of Medical Sciences, Moscow 125167, Russian Federation
Author Keywords Ferritin; Hyperfine interactions; Iron core; Iron-dextran complexes; Mössbauer spectroscopy
Chemicals/CAS Dextrans, 9004-54-0; Ferric Compounds; ferric oxide, 1309-37-1; Ferritins, 9007-73-2; Iron, 7439-89-6
Tradenames dextrafer, Leciva, Russian Federation; ferridextran; imferon, Benger, United States; imferon, Fisons, United Kingdom
Manufacturers Benger, United States; Fisons, United Kingdom; Leciva, Russian Federation
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Correspondence Address Oshtrakh, M.I.; Division of Applied Biophysics, Faculty of Physical Techniques, Ural State Technical University, Ekaterinburg 620002, Russian Federation; email: oshtrakh@mail.utnet.ru
CODEN IJBMD
PubMed ID 11718828
Language of Original Document English
Abbreviated Source Title Int. J. Biol. Macromol.
Source Scopus