Topic
Serum albumin
About: Serum albumin is a research topic. Over the lifetime, 16337 publications have been published within this topic receiving 516395 citations. The topic is also known as: blood albumin & ANALBA.
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TL;DR: Spectroscopic analysis of the emissionQuenching at different temperatures revealed that the quenching mechanism of serum albumin by dexamethasone is static quench mechanism.
Abstract: This study was designed to examine the interaction of dexamethasone (DEX) with bovine serum albumin (BSA) and human serum albumin (HSA) under physiological conditions with drug concentrations in the range of 2.5-20 microM and BSA/HSA was fixed at 5.0 microM. Spectroscopic analysis of the emission quenching at different temperatures revealed that the quenching mechanism of serum albumin by dexamethasone is static quenching mechanism. The binding sites number, n and binding constant, K were obtained at various temperatures. The distance r between dexamethasone and the protein was evaluated according to the theory of Foster energy transfer. The result of fluorescence spectra UV-vis absorption spectra and FT-IR spectra showed that the conformation of bovine serum albumin and human serum albumin has been changed in the presence of dexamethasone. The thermodynamic parameters, free energy change (DeltaG(0)), enthalpy change (DeltaH(0)) and entropy change (DeltaS(0)) for BSA-DEX and HSA-DEX were calculated according to van't Hoff equation and discussed.
202 citations
TL;DR: The adsorption of bovine serum albumin (BSA) onto hydroxyapatite (HA) has been studied as a function of protein concentration, pH and ionic strength, with results indicating that both electrostatic and hydration effects are important.
202 citations
TL;DR: The interactions of 3-carboxyphenoxathiin with BSA and HSA have been studied by fluorescence and circular dichroism spectroscopy, revealing a 1:1 interaction with a binding constant of about 105 M-1.
Abstract: The interactions of 3-carboxyphenoxathiin with Bovine Serum Albumin (BSA) and Human Serum Albumin (HSA) have been studied by fluorescence and circular dichroism spectroscopy. The binding of 3-carboxyphenoxathiin quenches the BSA and HSA fluorescence, revealing a 1:1 interaction with a binding constant of about 10(5) M(-1). In addition, according to the synchronous fluorescence spectra of BSA and HSA in presence of 3-carboxyphenoxathiin, the tryptophan residues of the proteins are most perturbed by the binding process. Finally, the distance between the acceptor, 3-carboxyphenoxathiin, and the donor, BSA or HSA, was estimated on the basis of the Forster resonance energy transfer (FRET). The fluorescence results are correlated with those obtained from the circular dichroism spectra, which reveal the change of the albumin conformation during the interaction process.
202 citations
TL;DR: Results demonstrated that LPL enzymatic activity and protein were removed from endothelial cells by triglyceride-rich lipoproteins (chylomicrons and VLDL).
202 citations
TL;DR: The present observations suggest that the two receptors cubilin and megalin are both involved in the endocytic uptake of albumin in renal proximal tubule cells.
201 citations