Protein affinity chromatography albumin

The ability of proteins to form enantioselective interactions with a large variety of drugs is used in chiral affinity chromatography. Protein CSPs that are most frequently used for the enantioseparation of pharmaceuticals include bovine serum albumin (BSA), human serum albumin... 

Procion Rubine MX-B, Procion Yellow H-A, and Turquoise MX-G. These dyes have found use over the last few decades in the purification of a broad range of proteins and enzymes, including albumin, decarboxylases, glycolytic enzymes, hydrolases, lyases, nucleases, oxidoreductases, synthetases, and transferases [77,78], The first use of dye-ligand affinity chromatography was described by Staal et al. in 1971 [79], Since that time, it has become an extremely popular tool for enzyme and protein purification, with hundreds of such compounds having been isolated by this technique [3-6,76-79],... 

Yatscoff RW, Tevaarwerk G), MacDonald JC. Quantification of nonenzymically glycated albumin and total serum protein by affinity chromatography. Clin Chem 1984 30 446-9. 

Fractionation of serum proteins was achieved by affinity chromatography three main selenium fractions corresponded to SeP, albumin and GPx. Mass balance performed under different experimental conditions showed quantitative selenium recovery. The distribution of selenium between plasma GPx ( 20%), SeP ( 55%) and albumin ( 20%) was similar in both populations... 

Hage, D.S. and Austin, J., High-performance affinity chromatography and immobilized serum albumin as probes for drug- and hormone-protein binding, J. Chromatogr. B, 739, 39, 2000. 

Plasma Proteome. The plasma proteome has been studied extensively. Plasma can be obtained readily from individuals by drawing blood using a simple procedure that is considered noninvasive. Plasma proteins have been characterized routinely by 2D gel followed by affinity chromatography, tandem mass spectroscopy, and comparison of protein sequence data in the protein databank. Some proteins such as albumin and transferrin, which are predominantly present in serum, are removed by affinity depletion chromatography to enrich the presence of other low-bundance proteins in plasma. More than 4000 proteins have been identified from human plasma, which are being developed to be used as a biomarker for several human diseases. 

Affinity chromatography has been used to isolate antigen-specific antibodies, hapten-specific antibodies, species-specific antibodies or to separate cross-reacting immunoglobulins from the antibody of interest. It has also been used to remove specific contaminants, e.g., serine proteases such as trypsin, thrombin, factor Xa or other contaminating proteins such as albumin. 

Many methods for the preparation of pure serum albumin are available, and some can be scaled down from techniques used by blood transfusion services to process protein components from outdated blood. Assay can be by affinity chromatography (GlOa), HPLG, isoelectric focusing, mobile affinity electrophoresis, and thiobarbituric acid photometry (NIO). The last method employed acid (pH 1) hydrolysis for 8 hours at 115°C to liberate the... 

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