The effect of lead cations on the fluorescence characteristics of bovine serum albumin in aqueous solution

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• 作者：I. A. Sergeeva (1)
  E. A. Shirshin (1)
  N. G. Zhdanova (2)
  V. V. Gibizova (1)
  G. P. Petrova (1)
  S. A. Kurguzenkov (2)
  V. V. Fadeev (1)
  
• 刊名：Optics and Spectroscopy
• 出版年：2013
• 出版时间：August 2013
• 年：2013
• 卷：115
• 期：2
• 页码：171-176
• 全文大小：226KB
• 参考文献：1. W. Dauer and S. Przedborski, Neuron ass="a-plus-plus">39, 889 (2003). <a class="external" href="http://dx.doi.org/10.1016/S0896-6273(03)00568-3">CrossRefa>
  2. K. Blennow, M. J. de Leon, and H. Zetterberg, Lancet ass="a-plus-plus">368, 387 (2006). <a class="external" href="http://dx.doi.org/10.1016/S0140-6736(06)69113-7">CrossRefa>
  3. L. V. Soustov, E. V. Chelnokov, N. M. Bityurin, V. V. Nemov, Yu. V. Sergeev, and M. A. Ostrovskii, Dokl. Akad. Nauk ass="a-plus-plus">388(5), 683 (2003).
  4. P. Rondeau, G. Navarra, V. Militello, and E. Bourdon, / Protein Aggregation, Ed. by D. A. Stein (Nova Science, 2010).
  5. G. P. Petrova, Yu. M. Petrusevich, and D. I. Ten, Quantum Electron. ass="a-plus-plus">32(10), 897 (2002). <a class="external" href="http://dx.doi.org/10.1070/QE2002v032n10ABEH002313">CrossRefa>
  6. G. Navarra, A. Tinti, M. Leone, V. Militello, and A. Torreggiani, J. Inorg. Biochem. ass="a-plus-plus">103, 1729 (2009). <a class="external" href="http://dx.doi.org/10.1016/j.jinorgbio.2009.09.023">CrossRefa>
  7. A. Stirpe, M. Pantusa, B. Rizzuti, L. Sportelli, R. Bartucci, and R. Guzzi, Int. J. Biological Macromolecules ass="a-plus-plus">49, 337 (2011). <a class="external" href="http://dx.doi.org/10.1016/j.ijbiomac.2011.05.011">CrossRefa>
  8. M. Bhattacharya, N. Jain, and S. Mukhopadhyay, J. Phys. Chem. B ass="a-plus-plus">115, 4195 (2011). <a class="external" href="http://dx.doi.org/10.1021/jp111528c">CrossRefa>
  9. N. El Kadi and N. Taulier, Biophys. J. ass="a-plus-plus">91, 3397 (2006). <a class="external" href="http://dx.doi.org/10.1529/biophysj.106.088963">CrossRefa>
  10. Peters. Theodore, / All About Albumin: Biochemistry, Genetics, and Medical Applications (Academic, San Diego, 1996).
  11. E. A. Permyakov, / Method of Intrinsic Luminescence of Protein (MGU, Moscow, 2003) [in Russian].
  12. H. LeVine, Protein Sci. ass="a-plus-plus">2(3), 404 (1993). <a class="external" href="http://dx.doi.org/10.1002/pro.5560020312">CrossRefa>
  13. A. A. Maskevich, V. I. Stsiapura, V. A. Kuzmitsky, I. M. Kuznetsova, O. I. Povarova, V. N. Uversky, and K. K. Turoverov, J. Proteome Res. ass="a-plus-plus">6, 1392 (2007). <a class="external" href="http://dx.doi.org/10.1021/pr0605567">CrossRefa>
  14. T. Otosu, E. Nishimoto, and S. Yamashita, J. Biochem. ass="a-plus-plus">147(2), 191 (2010). <a class="external" href="http://dx.doi.org/10.1093/jb/mvp175">CrossRefa>
  15. J. R. Lakowicz, / Principles of Fluorescence Spectroscopy (Kluwer Academic/Plenum, New York, 1999). <a class="external" href="http://dx.doi.org/10.1007/978-1-4757-3061-6">CrossRefa>
  16. K. N. Solov鈥檈v and E. A. Borisevich, Usp. Fiz. Nauk ass="a-plus-plus">175(3), 247 (2005). <a class="external" href="http://dx.doi.org/10.3367/UFNr.0175.200503b.0247">CrossRefa>
  17. L. V. Levshin and A. M. Saletskii, / Optical Methods of Molecular Systems (Moscow, 1994) [in Russian].
  18. P. Ragan and T. Turner, JAAPA: Offic. J. Amer. Acad. Physician Assist. ass="a-plus-plus">22(7), 40 (2009). <a class="external" href="http://dx.doi.org/10.1097/01720610-200907000-00010">CrossRefa>
  19. M. White, R. R. Kuntz, C. A. Ghiron, and W. A. Volkert, Photochem. Photobiol. ass="a-plus-plus">28(3), 413 (1978). <a class="external" href="http://dx.doi.org/10.1111/j.1751-1097.1978.tb07727.x">CrossRefa>
  20. M. Gonnelli and G. Strambini, Biochemistry ass="a-plus-plus">34(42), 13847 (1995). <a class="external" href="http://dx.doi.org/10.1021/bi00042a017">CrossRefa>
  21. A. A. Banishev, E. A. Shirshin, and V. V. Fadeev, Kvantovaya Elektron. ass="a-plus-plus">38(1), 76 (2008). <a class="external" href="http://dx.doi.org/10.1070/QE2008v038n01ABEH013654">CrossRefa>
  22. P. S. Sherin, O. A. Snytnikova, and Y. P. Tsentalovich, Chem. Phys. Lett. ass="a-plus-plus">391, 44 (2004). <a class="external" href="http://dx.doi.org/10.1016/j.cplett.2004.04.068">CrossRefa>
  23. B. Finstrom, F. Tfibel, and L. Lindqvist, Chem. Phys. Lett. ass="a-plus-plus">71(2), 312 (1981). <a class="external" href="http://dx.doi.org/10.1016/0009-2614(80)80172-2">CrossRefa>
  24. C. Pigault and D. Gerard, Photochem. Photobiol. ass="a-plus-plus">40(3), 291 (1984). <a class="external" href="http://dx.doi.org/10.1111/j.1751-1097.1984.tb04590.x">CrossRefa>
  
• 作者单位：I. A. Sergeeva (1)
  E. A. Shirshin (1)
  N. G. Zhdanova (2)
  V. V. Gibizova (1)
  G. P. Petrova (1)
  S. A. Kurguzenkov (2)
  V. V. Fadeev (1)
  
  1. Moscow State University, Moscow, 119991, Russia
  2. Kupala State University, ul. Ozheshko 22, Grodno, 230023, Belarus
  

文摘

The effect of lead (heavy metal) cations on the fluorescence characteristics and photophysical parameters (fluorescence intensity and anisotropy, absorption cross section, excited state lifetime, and rates of singlet-triplet conversion and reversible photobleaching) of tryptophan in an aqueous solution of bovine serum albumin (two-tryptophan protein) is studied and compared with the effect in the aqueous solution of tryptophan. It is demonstrated that the effect of lead on the fluorescence characteristics of the protein is manifested at a molar concentration ratio of metal cations and protein macromolecules of greater than 10 and related to the dynamic quenching of the excited state, protein aggregation, and an increase in the rate of singlet-triplet conversion (the effect of a heavy atom) in tryptophan molecules.