Thermodynamic parameters for binding of fatty acids to human serum albumin
نویسندگان
چکیده
منابع مشابه
Thermodynamic Analysis for Cationic Surfactants Binding to Bovine Serum Albumin
In the present study, the binding isotherms for interaction of a homologous series of n-alkyltrimethyl ammonium bromides with bovine serum albumin (BSA) have been analyzed on basis of intrinsic thermodynamic quantities. In this regards, the intrinsic Gibbs free energy of binding, AGb(i,)„ has been estimated at various surfactant concentrations and its trend of variation for both binding sets ha...
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Human serum albumin (HSA) is an important protein that carries variety of substances like some hormones and drugs in blood. Pharmacological studies of the interaction of many drugs and HSA are reported during several decades, specially recently years. Interaction of cortisol and fluoxetine hydrochloride (FLX) (as a common anti-stress drug) with HSA (as their carrier in blood) has been studied s...
متن کاملFluoxetin Competes with Cortisol for Binding to Human Serum Albumin
Human serum albumin (HSA) is an important protein that carries variety of substances like some hormones and drugs in blood. Pharmacological studies of the interaction of many drugs and HSA are reported during several decades, specially recently years. Interaction of cortisol and fluoxetine hydrochloride (FLX) (as a common anti-stress drug) with HSA (as their carrier in blood) has been studied s...
متن کاملthermodynamic analysis for cationic surfactants binding to bovine serum albumin
in the present study, the binding isotherms for interaction of a homologous series of n-alkyltrimethyl ammonium bromides with bovine serum albumin (bsa) have been analyzed on basis of intrinsic thermodynamic quantities. in this regards, the intrinsic gibbs free energy of binding, agb(i,)„ has been estimated at various surfactant concentrations and its trend of variation for both binding sets ha...
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In earlier studies on the binding of indole analogues with defatted human serum albumin (l), the intrinsic association constants for both a neutral ligand and a ligand bearing a negative charge were found to be invariant in the pH region of 5 to 10, implying that the structure of the binding site on the albumin did not change in this region. As the pH increased or decreased from this region the...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1990
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1990.tb15601.x