Search results for " Albumin"
showing 10 items of 320 documents
Femtosecond Transient Absorption Study of the Dynamics of Acrylodan in Solution and Attached to Human Serum Albumin
2003
The excited-state relaxation dynamics of the protein-labeling dye acrylodan in solution and attached to human serum albumin has been studied by femtosecond transient absorption spectroscopy. Time-resolved spectra and kinetics of stimulated emission and excited-state absorption in the wavelength region from 400 to 800 nm were studied in ethanol and dimethylformamide. The excited-state solvation dynamics is characterized by multiexponential behavior in both solvents. In ethanol solution, the time dependence of the transient spectra is interpreted in terms of fast solvent relaxation followed by excited-state isomerization of the dye. Acrylodan attached to the protein shows a relaxation compone…
Evaluation of enantioselective binding of antihistamines to human serum albumin by ACE.
2007
The drug binding to plasma and tissue proteins is a fundamental factor in determining the overall pharmacological activity of a drug. HSA, together with alpha(1)-acid glycoprotein, are the most important plasma proteins, which act as drug carriers, with implications on the pharmacokinetic of drugs. Among plasma proteins, HSA possesses the highest enantioselectivity. In this paper, a new methodology for the study of enantiodifferentiation of chiral drugs with HSA is developed and applied to evaluate the possible enantioselective binding of four antihistamines: brompheniramine, chlorpheniramine, hydroxyzine and orphenadrine to HSA. This study includes the determination of affinity constants o…
Displacement of phenprocoumon (Marcumar) from albumin by sulfonylurea compounds, suramin, and ioglycamic acid.
1972
The technique of Sephadex gel filtration was employed to characterize the effect of some sulfonylurea compounds, ioglycamic acid, and suramin on the binding of phenprocoumon to bovine serum albumin.
Characterization of antihistamine–human serum protein interactions by capillary electrophoresis
2007
An important topic in the drug discovery and development process is the role of drug binding to plasma proteins. In this paper the characterization of the interaction between antihistamines (cationic drugs) towards human serum albumin (HSA) and alpha(1)-acid glycoprotein (AGP) under physiological conditions by capillary electrophoresis-frontal analysis is presented. Furthermore, the binding of these drugs to all plasma proteins is evaluated by using ultrafiltration and capillary electrophoresis. Antihistamines present a wide-ranging behaviour with respect to their affinities towards plasma proteins. Orphenadrine, phenindamine, tripelenamine and tripolidine principally bind to HSA; carbinoxa…
Fast enantiomeric separation of propranolol by affinity capillary electrophoresis using human serum albumin as chiral selector: application to qualit…
2004
Abstract In the last years, capillary electrophoresis (CE) has gained considerable interest in pharmaceutical laboratories for controlling the chiral purity of drugs. This paper describes a simple and fast method for resolution of propranolol enantiomers by affinity capillary electrophoresis (ACE) using human serum albumin (HSA) as chiral selector. The effect of several experimental variables such as HSA concentration, temperature, chiral selector plug length and addition of organic modifiers, on the separation is evaluated. Complete enantioresolution of R- and S-propranolol was achieved in less than 5 min when the capillary was completely filled with 100 μM HSA solution and the electrophor…
Enrichment of proteinaceous materials on a strong cation-exchange diol silica restricted access material: protein–protein displacement and interactio…
2004
A study of size exclusion and enrichment of proteins employing strong cation-exchange diol silica restricted access material (SCX-RAM) under saturation conditions is presented. Experiments were carried out with bacitracin, protamine, ribonuclease, lysozyme and bovine serum albumin as individual proteinaceous analytes as well as comprehensive binary mixtures and with human urine samples. Protein size dependent capacity features of the SCX-RAM column was observed. Bacitracin demonstrated the highest capacity followed by protamine while adsorption capacities of both ribonuclease and lysozyme were found smaller by a factor of 10. Applying binary protein samples occurring displacement effects we…
Application of Liquid-Liquid Partition Chromatography (LLPC) in the Preparation of Steroid Binding Proteins
1989
Two human serum proteins, i.e. sex hormone binding globulin (h-SHBG) and corticosteroid binding globulin (h-CBG), rat corticosteroid binding globulin (r-CBG), and progesterone binding globulin (PBG) from new guinea pig were purified by the application of three different modes of chromatography. The proteins were purified by affinity chromatography and anion exchange chromatography. Fractions containing the steroid binding proteins were finally purified by liquid-liquid partition chromatography on LiParGel 750 (Merck, Darmstadt, FRG). This Chromatographic sequence clearly separated the steroid binding proteins from other proteins, mainly from serum albumin without a loss of protein and compl…
Versuche zur fraktionierung von proteingemischen mit polyacrylsäuren
1953
Proteine lassen sich quantitativ aus wasriger saurer Losung durch Polyacrylsauren (P 200–400) ausfallen. Die Symplexe losen sich bei neutralem PH; nach Entfernung der hochpolymeren Saure als schwerlosliches Ba- oder Protaminsalz werden die Proteine undenaturiert zuruckerhalten. Untersucht wurde die Abhangigkeit der ausgefallten Protein-menge vom PH und von der zugesetzten Menge an PAcs bei reinem Serum-Albumin und Globulin (Rind), sowie an Gemischen aus beiden und an Humanserum. Unter Verwendung der Papierelektrophorese konnte die bei allmahlicher Zugabe des Fallungsmittels bei PH 4, 6 eintretende Fraktionierung verfolgt werden, bei der zuerst Albumin, dann die Globuline zur Abscheidung gel…
Preferential solvation of lysozyme and bovine serum albumin in copper salt solutions. A quantitative chromatographic study
1986
Preferential solvation λ parameters for systems containing water-copper salt-protein (lysozyme or bovine serum albumin) have been determined by gel permeation chromatography. When water is preferentially adsorbed by the protein, good agreement is found between λ values determined by this method and by equilibrium dialysis-differential refractometry. The influence of the concentration and type of anion component of the copper salt, protein concentration and temperature has been investigated. The methodology used also allows direct visualization of the metal ion bound to the protein and to determine binding parameters. Apparent association constants of 2.0 × 102 M−1 and 1.7 × 102 M−1 have bee…
Adsorption of proteins on porous and non-porous poly(ethyleneimine) and tentacle-type anion exchangers
1990
Abstract Adsorption isotherms of proteins [bovine serum albumin (BSA), soybean trypsin inhibitor and alcohol dehydrogenase] on anion exchangers were measured by on-line and off-line methods. The poly(ethyleneimine) (PEI) type and the tentacle-type materials exhibited principally different modes of adsorption. On thin layers of PEI, bonded to non-porous silica, BSA adsorption data corresponded to a monolayer of molecules, with 80% adsorbed side-on, with a high affinity constant for binding, and 20% adsorbed more weakly. With porous material, the amount of BSA bound per unit surface with high affinity was smaller. With tentacle-type anion exchangers, adsorption exceeded a monolayer by far, an…