Magnetic Birefringence Study of the Magnetic Core Structure of Ferritin

• Authors: M. Koralewski , M. Pochylski , Z. Mitróová , L. Melníková , J. Kováč , M. Timko , P. Kopčanský
• Languages of publication: EN

Abstracts

EN

Magnetically induced optical birefringence (Δ n) was measured for magnetoferritin and horse spleen ferritin aqueous suspensions. The Δ n for magnetoferritin was described in the frame of the Langevin formalism taking into account distribution of core diameter. The established average magnetic dipole moment and core diameter is equal to about 460 μ_{B} and 3 nm, respectively. It was shown that magnetic birefringence and the Cotton-Mouton constant can be powerful parameters in identification of the magnetic core structure of ferritin, especially useful in biomedicine.

Keywords

EN

78.20.Ls; 87.15.-v; 87.85.jf

Discipline

• 78.20.Ls: Magneto-optical effects(for magneto-optical devices, see 85.70.Sq)
• 87.15.-v: Biomolecules: structure and physical properties(for NMR of biomolecules, see 82.56.Pp)
• 87.85.jf: Bio-based materials

• Publisher: Institute of Physics, Polish Academy of Sciences
• Journal: Acta Physica Polonica A
• Year: 2012
• Volume: 121
• Issue: 5-6
• Pages: 1237-1239

Dates

published

2012-05

Contributors

author

M. Koralewski

• Faculty of Physics, Adam Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland

author

M. Pochylski

• Faculty of Physics, Adam Mickiewicz University, Umultowska 85, 61-614 Poznań, Poland

author

Z. Mitróová

• Institute of Experimental Physics, SAS, Watsonova 47, 040 01 Kosice, Slovakia

author

L. Melníková

• Institute of Experimental Physics, SAS, Watsonova 47, 040 01 Kosice, Slovakia

author

J. Kováč

• Institute of Experimental Physics, SAS, Watsonova 47, 040 01 Kosice, Slovakia

author

M. Timko

• Institute of Experimental Physics, SAS, Watsonova 47, 040 01 Kosice, Slovakia

author

P. Kopčanský

• Institute of Experimental Physics, SAS, Watsonova 47, 040 01 Kosice, Slovakia

References

• 1. F.C. Meldrum, B.R. Heywood, S. Mann, Science 257, 522 (1992)
• 2. M. Uchida, S. Kang, C. Reichardt, K. Harlen, T. Duglas, Biochim. Biophys. Acta 1800, 834 (2010)
• 3. M.T. Klem, J. Mosolf, M. Young, T. Douglas, Inorg. Chem. 47, 2237 (2008)
• 4. I. Yamashita, K. Iwahori, S. Kumagai, Biochim. Biophys. Acta 1800, 846 (2010)
• 5. K. Ohara, Y. Uraoka, T. Fuyuki, I. Yamashita, T. Yaegashi, M. Moniwa, M. Yoshimaru, Jpn. J. Appl. Phys. 48, 04C153 (2009)
• 6. J.L. Kirschvink, A. Kobayashi-Kirschvink, B.J. Woodford, Proc. Natl. Acad. Sci. USA 89, 7683 (1992)
• 7. C. Quintana, Mini-Rev. Med. Chem. 7, 961 (2007)
• 8. V.C. Jordan, M.R. Caplan, K.M. Bennett, Magn. Res. Med. 64, 1260 (2010)
• 9. A. Figuerola, R. Di Corato, L. Manna, T. Pellegrino, Pharmacol. Res. 62, 126 (2010)
• 10. M. Koralewski, M. Pochylski, Z. Mitróová, M. Timko, P. Kopčanský, L. Melníková, J. Magn. Magn. Mater. 323, 2413 (2011)
• 11. Z. Mitróová, L. Melníková, J. Kováč, M. Timko, P. Kopčanský, Acta Phys. Pol. A 121, 1318 (2012)
• 12. M. Koralewski, M. Pochylski, J. Gierszewski, J. Magn. Magn. Mater. 323, 1140 (2011)
• 13. C.T. O'Konski, T. Yoshioka, W.H. Orttung, J. Phys. Chem. 63, 1558 (1959)
• 14. E. Hassamony, E. Dubois, J.-C. Bacri, R. Perzynski, Yu.L. Raikher, V.I. Stepanov, Eur. Phys. J. B 5, 859 (1989)
• 15. P.C. Scholten, IEEE Trans. Magn. 11, 1400 (1975)
• 16. U. Neitzel, K. Barner, Phys. Lett. A 63, 327 (1977)
• 17. J. Popplewell, L. Sakhnini, J. Magn. Magn. Mater. 149, 72 (1995)
• 18. H. Mouton, Int. Crit. Tables 7, 109 (1934)
• 19. M. Pankowska, A. Dobek, J. Chem. Phys. 131, 015105 (2009)

Identifiers

DOI

10.12693/APhysPolA.121.1237