منابع مشابه
Fluoxetin 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 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 کاملProbing the Binding of Valacyclovir Hydrochloride to the Human Serum Albumin
UV-visible and Fluorescence spectroscopic methods were employed to study the interaction of human serum albumin (HSA) with Valacyclovir Hydrochloride. Additionally, molecular dynamics and molecular docking simulations were used to visualize and specify the binding site of Valacyclovir Hydrochloride. The Stern-Volmer and van't Hoff equations along with spectroscopic observations, were used to de...
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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ژورنال
عنوان ژورنال: RADIOISOTOPES
سال: 1977
ISSN: 1884-4111,0033-8303
DOI: 10.3769/radioisotopes.26.8_525