Bulletin of the Korean Chemical Society

  • 제29권4호
  • /
  • Pages.736-740
  • /
  • 2008
  • /
  • 0253-2964(pISSN)
  • /
  • 1229-5949(eISSN)
대한화학회 (Korean Chemical Society)
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A Thermodynamic Study on the Binding of Cobalt Ion with Myelin Basic Protein

  • Behbehani, G. Rezaei (Chemistry Department, Imam Khomeini International University) ;
  • Saboury, A.A. (Institute of Biochemistry and Biophysics, University of Tehran) ;
  • Baghery, A. Fallah (Chemistry Department, Imam Khomeini International University)
  • 발행 : 2008.04.20
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초록

The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent calcium ion was studied by isothermal titration calorimetry at 27 ${^{\circ}C}$ in aqueous solution. The extended solvation model was used to reproduce the enthalpies of $Co^{2+}$-MBP interaction over the whole $Co^{2+}$ concentrations. The solvation parameters recovered from the solvation model were attributed to the structural change of MBP due to the metal ion interaction. It was found that there is a set of three identical and noninteracting binding sites for $Co^{2+}$ ions. The association equilibrium constant is 0.015 ${\mu}M^{-1}$. The molar enthalpy of binding is $\Delta$H = −14.60 kJ $mol^{-1}$.

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참고문헌

  1. Saboury, A. A. J. Therm. Anal. Cal. 2003, 72, 93-103 https://doi.org/10.1023/A:1023955300221
  2. Saboury, A. A. J. Therm. Anal. Cal. 2004, 77, 997-1004 https://doi.org/10.1023/B:JTAN.0000041675.76664.07
  3. Ataie, G.; Moosavi-Movahedi, A. A.; Saboury, A. A.; Hakimelahi, G. H.; Ru. Hwu, J.; Tsay, S. C. International Journal of Biological Macromolecule 2000, 27, 29-33 https://doi.org/10.1016/S0141-8130(99)00113-0
  4. Saboury, A. A. J. Iran Chem. Soc. 2006, 3, 1-21 https://doi.org/10.1007/BF03245784
  5. Saboury, A. A.; Dahut, M. U.; Ghobadi, S.; Chamani, J.; Moosavi-Movahedi, A. A. J. Chin. Chem. Soc. 1998, 45, 667 https://doi.org/10.1002/jccs.199800101
  6. Bathaie, S. Z.; Moosavi-Movahedi, A. A.; Saboury, A. A. Nuc. Acid Res. 1999, 27, 1001 https://doi.org/10.1093/nar/27.4.1001
  7. Housaindokht, M. R.; Chamani, J.; Saboury, A. A.; Moosavi- Movahedi, A. A. Bull. Kor. Chem. Soc. 2001, 22, 145
  8. Arabzadeh, A.; Bathaie, S. Z.; Farsam, H.; Amanlou, M.; Saboury, A. A.; Moosavi-Movahedi, A. A. Inter. J. Pharmac. 2002, 237, 47 https://doi.org/10.1016/S0378-5173(02)00020-0
  9. Ataie, G.; Moosavi-Movahedi, A. A.; Saboury, A. A.; Hakimelahi, G. H.; Ru. Hwu, J.; Tsay, S. C. Int. J. Biol. Macromol. 2000, 27, 29 https://doi.org/10.1016/S0141-8130(99)00113-0
  10. Saboury, A. A.; Karbassi, F. Thermochimica Acta 2000, 362, 121 https://doi.org/10.1016/S0040-6031(00)00579-7
  11. Mahmoudi, A.; Nazari, K.; Moosavi-Movahedi, A. A.; Saboury, A. A. Thermochim. Acta 2002, 385, 33 https://doi.org/10.1016/S0040-6031(01)00689-X
  12. Ajloo, D.; Moosavi-Movahedi, A. A.; Hakimelahi, G. H.; Saboury, A. A.; Gharibi, H. Coll. Surf. B: Biointerfaces 2002, 26, 185 https://doi.org/10.1016/S0927-7765(02)00003-6
  13. Saboury, A. A. Biologia 2002, 57, 221
  14. Bathaie, S. Z.; Moosavi-Movahedi, A. A.; Ranjbar, B.; Saboury, A. A. Coll. Surf. B: Biointerfaces 2003, 28, 17 https://doi.org/10.1016/S0927-7765(02)00128-5
  15. Chamani, J.; Moosavi-Movahedi, A. A.; Saboury, A. A.; Gharanfoli, M.; Hakimelahi, G. H. J. Chem. Thermodyn. 2003, 35, 199 https://doi.org/10.1016/S0021-9614(02)00312-9
  16. Bordbar, A. K.; Ghaderi, A. R.; Safaei, E.; Tangestaninejad, S.; Saboury, A. A.; Moosavi-Movahedi, A. A. Bull. Kor. Chem. Soc. 2003, 24, 547 https://doi.org/10.5012/bkcs.2003.24.5.547
  17. Mansoori Torshizi, H.; Eslami Moghaddam, M.; Saboury, A. A. Acta Biochim. Biophys. Sin. 2003, 35, 886
  18. Gharanfoli, A.; Moosavi-Movahedi, A. A.; Safarian, S.; Chamani, J.; Saboury, A. A. Thermochim. Acta 2004, 411, 37 https://doi.org/10.1016/j.tca.2003.07.008
  19. Moosavi-Movahedi, A. A.; Golchin, A. R.; Nazari, K.; Chamani, J.; Saboury, A. A.; Bathaie, S. Z.; Tangestaninejad, S. Thermochim. Acta 2004, 414, 233 https://doi.org/10.1016/j.tca.2004.01.007
  20. Nazari, K.; Golchin, A. R.; Moosavi-Movahedi, A. A.; Saboury, A. A.; Hakimelahi, G. H.; Shokravi, A.; Tangestani-Nejad, S. Thermochim. Acta 2005, 428, 157 https://doi.org/10.1016/j.tca.2004.10.008
  21. Sarraf, N. S.; Mamaghani-Rad, S.; Karbassi, F.; Saboury, A. A. Bull. Kor. Chem. Soc. 2005, 26, 1051 https://doi.org/10.5012/bkcs.2005.26.7.1051
  22. Saboury, A. A.; Bordbar, A. K.; Moosavi-Movahedi, A. A. Bull. Chem. Soc. Jpn. 1996, 69, 3031 https://doi.org/10.1246/bcsj.69.3031
  23. Saboury, A. A.; Bordbar, A. K.; Moosavi-Movahedi, A. A. J. Chem. Thermodyn. 1996, 28, 1077 https://doi.org/10.1006/jcht.1996.0092
  24. Nazari, K.; Moosavi-Movahedi, A. A.; Saboury, A. A. Thermochim. Acta 1997, 302, 131 https://doi.org/10.1016/S0040-6031(97)00211-6
  25. Moosavi-Movahedi, A. A.; Saboury, A. A. Jour. Chem. Soc. Pak. 1999, 21, 248
  26. Saboury, A. A.; Shamsaei, A. A.; Moosavi-Movahedi, A. A.; Mansori-Torshizi, H. Chin. Chem. Soc. 1999, 46, 917 https://doi.org/10.1002/jccs.199900125
  27. Saboury, A. A.; Atri, M. S.; Sanati, M. H.; Sadeghi, M. J. Therm. Ana. Cal. 2006, 83, 175-179 https://doi.org/10.1007/s10973-005-6954-7
  28. Saboury, A. A.; Atri, M. S.; Sanati, M. H.; Moosavi-Movahedi, A. A.; Hakimelahi, G. H.; Sadeghi, M. Biopolymers 2006, 81, 120-126 https://doi.org/10.1002/bip.20386
  29. Saboury, A. A.; Atri, M. S.; Sanati, M. H.; Moosavi-Movahedi, A. A.; Haghbeen, K. Int. J. Biol. Macromol. 2005, 36, 305-309 https://doi.org/10.1016/j.ijbiomac.2005.07.003
  30. Saboury, A. A.; Kordbacheh, M.; Sanati, M. H.; Mizani, F.; Shamsipur, M.; Yakhchali, M. B.; Moosavi-Movahedi, A. A. Asian J. Chem. 2005, 17, 2773-2782
  31. Atri, M. S.; Saboury, A. A.; Rezaei-Tavirani, M.; Sanati, M. H.; Moosavi-Movahedi, A. A.; Sadeghi, M.; Mansuri-Torshizi, H.; Khodabandeh, N. Thermochim. Acta 2005, 438, 178-184 https://doi.org/10.1016/j.tca.2005.08.033
  32. Saboury, A. A.; Ghourchaei, H.; Sanati, M. H.; Atri, M. S.; Rezaei-Tawirani, M.; Hakimelahi, G. H. J. Therm. Ana. Cal. 2006, 83, 175-179 https://doi.org/10.1007/s10973-005-6954-7
  33. Hindmarsh, P. C.; Brook, C. G. Br. Med. J. (Clin. Res. Ed.) 1987, 295, 573-583 https://doi.org/10.1136/bmj.295.6598.573
  34. de Voc, A. M.; Ultsch, M.; Kossiakoff, A. A. Science 1992, 255, 306-402 https://doi.org/10.1126/science.1549776
  35. Filikov, A. V.; Hayes, R. J.; Luo, P.; Stark, D. M.; Chan, C.; Kundu, A.; Dahiyat, B. I. Protein Sci. 2002, 11, 1452-1461 https://doi.org/10.1110/ps.3500102
  36. Saboury, A. A.; Sarri-Sarraf, N.; Saeidian, S. J. Termochim. Acta 2002, 381, 147-151 https://doi.org/10.1016/S0040-6031(01)00654-2
  37. Saboury, A. A. J. Therm. Analysil. Calorimetry 2004, 77, 1004-1010
  38. Umar Dahot, M.; Saboury, A. A.; Moosavi-Movahedi, A. A. J. Inhibition. Medicinal. Chemistry 2004, 19, 157-160 https://doi.org/10.1080/14756360310001650255
  39. Divsalar, A.; Saboury, A. A.; Yousefi, R.; Moosavi-Movahedi, A. A.; Mansoori-Torshizi, A. International Journal of Biological Macromolecules 2007, 40, 381-386 https://doi.org/10.1016/j.ijbiomac.2006.09.015
  40. Saboury, A. A. J. Chem. Termodynamics 2003, 35, 1975-1981 https://doi.org/10.1016/j.jct.2003.08.006
  41. Sarraf, N. S.; Mamaghani-Rad, S.; Karbassi, F.; Saboury, A. A. Bull. Korean Chem. Soc. 2005, 26, 1051 https://doi.org/10.5012/bkcs.2005.26.7.1051
  42. Rezaei Behbehani, G. J. Bull. Korean Chem. Soc. 2005, 2, 238-240 https://doi.org/10.5012/bkcs.2005.26.2.238
  43. Rezaei Behbehani, G. Acta Chimica Slov. 2005, 52, 282-285
  44. Rezaei Behbehani, G.; Tazikeh, E.; Saboury, A. A. J. Bull. Korean Chem. Soc. 2006, 2, 208-210 https://doi.org/10.5012/bkcs.2006.27.2.208
  45. Rezaei Behbehani, G.; Ghamamy, S. 2006, 444, 71-76 https://doi.org/10.1016/j.tca.2006.02.028
  46. Rezaei Behbehani, G.; Ghamamy, S.; Waghorne, W. E. J. Thermochimica Acta 2006, 448, 37-42 https://doi.org/10.1016/j.tca.2006.06.021
  47. Rezaei Behbehani, G.; Tazikeh, E.; Saboury, A. A. Acta Chimica Slov. 2006, 53, 363-369
  48. Rezaei Behbehani, G.; Saboury, A. A. J. Thermochimica Acta 2007, 452, 76-79 https://doi.org/10.1016/j.tca.2006.10.024
  49. Carnegie, P. R.; Moore, W. J.; Myelin Basic Protein in Proteins of the Nervous System, 2nd Ed.; Bradshaw, R. A.; Schneider, D. M., Eds.; Raven, New York, 1980
  50. Lintner, R. N.; Dyer, C. A. J. Neurosci. Res. 2000, 60, 437-449 https://doi.org/10.1002/(SICI)1097-4547(20000515)60:4<437::AID-JNR2>3.0.CO;2-9
  51. Rezaei Behbehani, G.; Dillon, M.; Smyth, J.; Waghorne, W. E. J. Solution Chem. 2002, 31, 811-822 https://doi.org/10.1023/A:1021397327617
  52. Reza Bebahani, G.; Dunnion, D.; Falvey, P.; Hickey, K.; Meade, M.; McCarthy, Y.; Symons, M. C. R.; Waghorne, W. E. J. Solution Chem. 2000, 29, 521-539 https://doi.org/10.1023/A:1005142112945
  53. Costigan, A.; Feakins, D.; McStravick, Ita.; O'Duinn, C.; Ryan, J.; Waghorne, W. E. J. Chem. Soc. Faraday Trans. 1991, 87, 2443-2446 https://doi.org/10.1039/ft9918702443
  54. Feakins, D.; O'Neill, R. D.; Waghorne, W. E. J. Chem. Soc. Faraday Trans. 1983, 79, 2289-2298 https://doi.org/10.1039/f19837902289
  55. Saboury, A. A. Journal of Thermal Analysis and Calorimetry 2003, 72, 93-103 https://doi.org/10.1023/A:1023955300221
  56. Saboury, A. A. Journal of the Iranian Chemical Society 2006, 3, 1-21 https://doi.org/10.1007/BF03245784
  57. Whitaker, J. N.; Mitchell, G. W. Ann. Neurol. 1996, 40, 3-4 https://doi.org/10.1002/ana.410400103
  58. Smith, R. J. Neurochem. 1992, 59, 1589-1608 https://doi.org/10.1111/j.1471-4159.1992.tb10989.x
  59. Pritzker, L. B.; Joshi, S.; Gowan, J. J.; Harauz, G.; Moscarello, M. A. Biochemistry 2000, 39, 5374-5381 https://doi.org/10.1021/bi9925569
  60. Nowak, M. W.; Berman, H. A. Biochemistry 1991, 30, 7642-7651 https://doi.org/10.1021/bi00244a037
  61. Moscarello, M. A.; Wood, D. D.; Ackerley, C.; Boulias, C. J. Clin. Invest. 1994, 94, 146-154 https://doi.org/10.1172/JCI117300
  62. Palma, A. E.; Owh, P.; Fredric, C.; Readhead, C.; Moscarello, M. A. J. Neurochem. 1997, 69, 1753-1762 https://doi.org/10.1046/j.1471-4159.1997.69041753.x

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