Thermodynamic Studies of Myelin Basic Protein upon Interaction with Zinc | Zendy

Saboury Ali Akbar | Zendy; Saeidian Shahriar | Zendy; Sanati Mohammad Hosain | Zendy; MoosaviMovahedi Ali Akbar | Zendy; Alasti Fatameh | Zendy

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Thermodynamic Studies of Myelin Basic Protein upon Interaction with Zinc

Author(s) -

Saboury Ali Akbar,

Saeidian Shahriar,

Sanati Mohammad Hosain,

MoosaviMovahedi Ali Akbar,

Alasti Fatameh

Publication year - 2001

Publication title -

journal of the chinese chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.329

H-Index - 45

eISSN - 2192-6549

pISSN - 0009-4536

DOI - 10.1002/jccs.200100119

Subject(s) - chemistry , isothermal titration calorimetry , zinc , titration , spectrophotometry , dissociation constant , divalent , endothermic process , myelin basic protein , calorimetry , tris , binding constant , scatchard plot , inorganic chemistry , chromatography , binding site , biochemistry , myelin , organic chemistry , thermodynamics , central nervous system , receptor , physics , adsorption , neuroscience , biology

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 (ΔH = + 159 kJ mol −1 ) with a dissociation binding constant of 0.445 μM. 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.

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