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

被引：7

作者：

Behbehani, G. Rezaei ^{[1
,3
]}

Saboury, A. A. ^{[2
]}

Sarvestani, S. Tahmasebi ^{[3
]}

Mohebbian, M. ^{[3
]}

Payehghadr, M. ^{[3
,4
]}

Abedini, J. ^{[3
]}

机构：

[1] Imam Khomeini Int Univ, Dept Chem, Qazvin, Iran

[2] Univ Tehran, Inst Biochem & Biophys, Tehran, Iran

[3] PNU, Dept Chem, Abhar, Iran

[4] PNU, Dept Chem, Karaj, Iran

来源：

JOURNAL OF THERMAL ANALYSIS AND CALORIMETRY | 2010年 / 102卷 / 02期

关键词：

Human serum albumin; Isothermal titration calorimetry; Theophylline; Binding sites; ISOTHERMAL TITRATION CALORIMETRY; HIGH-PERFORMANCE METHOD; PLASMA-PROTEIN-BINDING; MAGNESIUM-ION; LIGAND-BINDING; DRUG; LYSOZYME; ENTHALPY; AFFINITY;

D O I：

10.1007/s10973-010-0694-z

中图分类号：

O414.1 [热力学];

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 A degrees 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 (K (d)), the molar enthalpy of binding (Delta Iu) and other thermodynamic parameters can be obtained by the extended solvation theory.

引用

页码：793 / 798

页数：6

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