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A calorimetric study on the interaction between Vitamin-B6 and lysozyme

Author Affiliations

  • 1Chemistry Department, Azad Takestan University, Qazvin, IRAN
  • 2Chemistry Department, Payam Noor University, Abhar, IRAN
  • 3Chemistry Department, Imam Khomeini International University, Qazvin, IRAN

Res. J. Recent Sci., Volume 1, Issue (ISC-2011), Pages 345-347,(2012)


The binding reaction between vitamin B6 (B6, pyridoxine) and lysozyme (Lys) was investigated for the first time by isothermal titration calorimetry (ITC), at pH 7 at 27C in tris buffer (25mmol.L-1). The enthalpies of LYS+B6 interaction are reported and analysed in term of the extended solvation model. The thermodynamic parameters, enthalpy changes (ΔH) and entropy changes(ΔS) were calculated. These data suggested that hydrophobic interaction was the predominant intermolecular forces stabilizing the complex, which was in good agreement with the results of molecular modeling study. It was found that LYS has one non-cooperativebinding site for Vitamin B6.


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