Topic
Human serum albumin
About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.
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TL;DR: Warfarin and phenprocoumon binding to human serum albumin was studied by equilibrium dialysis to establish an understanding of the mechanism of action of these drugs.
Abstract: Warfarin and phenprocoumon binding to human serum albumin was studied by equilibrium dialysis. The first stoichiometric binding constant was 1.89 x 10(5) M-1 for warfarin and 2.40 x 10(5) M-1 for phenprocoumon. The affinity of warfarin was markedly increased on addition of up to 3 mol mol-1 albumin of palmitic, stearic, oleic or linoleic acids with energetic couplings for co-binding of one molecule of each of the fatty acids and one molecule of warfarin of 0.9, 1.1, 0.7 and 0.6 kJ mol-1, respectively. The affinity of phenprocoumon was only increased slightly on addition of palmitate with an energetic coupling of 0.3 kJ mol-1. Six consecutive serum samples were obtained from each of 14 patients undergoing surgery. The serum affinity of the drugs varied considerably corresponding to free drug concentrations between 0.7 and 2.7% for warfarin and between 0.8 and 4.9% for phenprocoumon. The affinity of warfarin but not of phenprocoumon was correlated to the increasing plasma fatty acid concentration. Anticoagulant therapy with phenprocoumon may thus be less sensitive than warfarin to changes in the fatty acid concentration of plasma.
87 citations
TL;DR: Synchronous fluorescence and CD spectra of HSA revealed that the binding of DCP to HSA did not cause a significant conformational change in protein, but the interaction of DQ with HSA led to an alteration in the protein structure.
87 citations
TL;DR: To test the efficiency of HSA removal from human serum, proteins in the serum and eluted portion were analyzed by two-dimensional gel electrophoresis and the depletion efficiencies for HSA were above 87% for all studied concentrations.
87 citations
TL;DR: In this article, the binding to a biological macromolecule (human serum albumin, HSA) of small molecules (two drugs: warfarin and furosemide) has been studied by hig-performance liquid chromatography.
87 citations
TL;DR: Photon correlation spectroscopy and laser doppler anenometry showed that the coating reduced the adsorption of the protein to the polystyrene microspheres surface, which confirmed that the hydrophilic polyoxyethylene steric layer, created by coating with the block copolymers, reduced the advertisers of human serum albumin.
87 citations