A thermodynamic study on the binding of theophylline with human serum albumin

被引：0
|
作者：
G. Rezaei Behbehani
A. A. Saboury
S. Tahmasebi Sarvestani
M. Mohebbian
M. Payehghadr
J. Abedini
机构：
[1] Imam Khomeini International University,Chemistry Department
[2] University of Tehran,Institute of Biochemistry and Biophysics
[3] Payame Noor University (PNU),Chemistry Department
[4] Payame Noor University (PNU),Chemistry Department
来源：
Journal of Thermal Analysis and Calorimetry | 2010年 / 102卷
关键词：
Human serum albumin; Isothermal titration calorimetry; Theophylline; Binding sites;
D O I：
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中图分类号：
学科分类号：
摘要：
The thermodynamic parameters of interaction between theophylline and Human Serum Albumin (HSA) in buffer solution (30 mM) of pH = 7 at 27 °C was investigated by isothermal titration calorimetry (ITC). The thermodynamic quantities of the binding mechanism, the number of binding sites (g), the dissociation binding constant (Kd), the molar enthalpy of binding (ΔΗ) and other thermodynamic parameters can be obtained by the extended solvation theory.
引用
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页码：793 / 798
页数：5
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