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: Unlike the usually employed thiobarbituric acid assay the present procedure is truly specific for the detection of ketoamine linkages of glycosylated proteins.
Abstract: A specific and sensitive method for quantification of the fructose-lysine linkages present in non-enzymatically glycosylated albumin and other proteins is described. Protein is hydrolyzed for 18 h in 6 mol/l HCl at 95 degrees C to yield furosine (epsilon-N-(2-furoylmethyl)-L-lysine) known as a specific degradation product of fructose-lysine. Furosine is then separated on HPLC and quantified by its UV-absorbance against a prepared fructose-lysine standard. The method has been successfully used for the determination of glycosyl-albumin in diabetic patients starting from 100 microliter serum or less, as well as for various other proteins. Unlike the usually employed thiobarbituric acid assay the present procedure is truly specific for the detection of ketoamine linkages of glycosylated proteins.
122 citations
TL;DR: Results suggest that serum albumin acts as a major and predominate antioxidant exerting a glutathione-linked thiol peroxidase activity which removes reactive oxygen species such as H2O2 within blood plasma.
122 citations
TL;DR: All-atom molecular dynamics simulations of albumin were carried out to understand how electrostatics can affect the conformation of a single albumin molecule just prior to self-assembly and suggested that hydrophobic attractions and counterion binding may be strong enough to effectively overcome the electrostatic repulsions between the highly charged monomers.
Abstract: A better understanding of protein aggregation is bound to translate into critical advances in several areas, including the treatment of misfolded protein disorders and the development of self-assembling biomaterials for novel commercial applications. Because of its ubiquity and clinical potential, albumin is one of the best-characterized models in protein aggregation research; but its properties in different conditions are not completely understood. Here, we carried out all-atom molecular dynamics simulations of albumin to understand how electrostatics can affect the conformation of a single albumin molecule just prior to self-assembly. We then analyzed the tertiary structure and solvent accessible surface area of albumin after electrostatically triggered partial denaturation. The data obtained from these single protein simulations allowed us to investigate the effect of electrostatic interactions between two proteins. The results of these simulations suggested that hydrophobic attractions and counterion binding may be strong enough to effectively overcome the electrostatic repulsions between the highly charged monomers. This work contributes to our general understanding of protein aggregation mechanisms, the importance of explicit consideration of free ions in protein solutions, provides critical new insights about the equilibrium conformation of albumin in its partially denatured state at low pH, and may spur significant progress in our efforts to develop biocompatible protein hydrogels driven by electrostatic partial denaturation.
122 citations
TL;DR: The sulfhydryl groups in chicken ovalbumin, bovine β-lactoglobulin, and Bovine serum albumin were studied with four different types of chemical reagents: p-chloromercuribenzoate, iodine, N-ethylmaleimide and 5,5′-dithiobis (2-nitrobenzoic acid) as mentioned in this paper.
122 citations
TL;DR: Sustained-release systems were made by incorporating bovine serum albumin and magnetic steel beads in an ethylene-vinyl acetate copolymer matrix, resulting in corresponding increases and decreases in release and establishing a pattern of modulated sustained release.
Abstract: Sustained-release systems were made by incorporating bovine serum albumin and magnetic steel beads in an ethylene-vinyl acetate copolymer matrix. When exposed to aqueous medium, the polymer matrix released the albumin slowly and continuously. Application of an oscillating magnetic field increased the release rate by as much as 100%. Intervals of 6-hr periods of magnetic exposure and nonexposure were alternated over a 5-day period, resulting in corresponding increases and decreases in release and establishing a pattern of modulated sustained release.
122 citations