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: A hypothesis of a steady state of liver heme metabolism, controlled by the concentration of "free" heme, is presented and the different effects of heme on the synthesis of a number of proteins are summarized.
286 citations
TL;DR: Micropolarities in the two proteinous environments have been determined following the polarity sensitivity of the CT emission and addition of urea to the protein-bound systems leads to a reduction in the fluorescence anisotropy indicating the denaturation of the proteins.
Abstract: Interaction of 3-acetyl-4-oxo-6,7-dihydro-12H indolo-[2,3-a] quinolizine (AODIQ), a biologically active molecule, with model transport proteins, bovine serum albumin (BSA) and human serum albumin (HSA) have been studied using steady state and picosecond time-resolved fluorescence and fluorescence anisotropy. The polarity dependent intramolecular charge transfer (ICT) process is responsible for the remarkable sensitivity of this biological fluorophore to the protein environments. The CT fluorescence exhibits appreciable hypsochromic shift along with an enhancement in the fluorescence yield, fluorescence anisotropy (r) and fluorescence lifetime upon binding with the proteins. The reduction in the rate of ICT within the hydrophobic interior of albumins leads to an increase in the fluorescence yield and lifetime. Marked increase in the fluorescence anisotropy indicates that the probe molecule is located in a motionally constrained environment within the proteins. Micropolarities in the two proteinous environments have been determined following the polarity sensitivity of the CT emission. Addition of urea to the protein-bound systems leads to a reduction in the fluorescence anisotropy indicating the denaturation of the proteins. Polarity measurements and fluorescence resonance energy transfer (FRET) studies throw light in assessing the location of the fluorophore within the two proteinous media.
286 citations
TL;DR: Several compounds showed stronger HSA binding than can be expected from their lipophilicity alone, and comparison between predicted and experimental binding affinity allows the identification of compounds that have good complementarities with any of the known binding sites.
285 citations
TL;DR: The acrylamide quenching reaction is shown to be very discriminating in sensing the exposure of fluorescing tryptophanyl residues in globular proteins, and these parameters characterize the nature of the protein matrix enveloping the fluorophors.
Abstract: The acrylamide quenching reaction is shown to be very discriminating in sensing the exposure of fluorescing tryptophanyl residues in globular proteins. The quenching rate constants for some proteins, such as aldolase and human serum albumin, are reported to be independent of the solvent viscosity, indicating that the reaction is limited by penetration of the quencher through the protein matrix. Temperature-dependent studies are performed to determine the activation energy and entropy for the penetration of acrylamide into these proteins. The tryptophanyl residues in aldolase are shown to be shielded by a large activation energy barrier, while the single residue in human serum albumin is shielded by a large activation entropy barrier. These parameters characterize the nature of the protein matrix enveloping the fluorophors.
285 citations
285 citations