- 作者: Ali Akbar Sabourya, Shahriar Saeidiana, Mohammad Hosain Sanatib, Ali Akbar Moosavi-Movahedia and Fatameh Alastib
- 中文摘要:
aInstitute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
bThe National Research Center of Genetic Engineering and Biotechnology, Tehran, Iran
The interaction of myelin basic protein (MBP) from bovine central nervous system with divalent zinc ion was studied by UV-Vis titration spectrophotometry and isothermal titration calorimetry techniques at 27 °C in Tris buffer solution at pH = 7.2. MBP has one binding site for a zinc ion. The binding of a zinc ion is endothermic (DH = +159 kJ mol-1) with a dissociation binding constant of 0.445 mM. The results obtained by two previous methods of isothermal titration spectrophotometry and calorimetry are similar and consistent with the result obtained from a new calculation method of calorimetric data analysis according to the Scatchard plot. - 英文摘要: --
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