Search results for "Bovine Serum Albumin"
showing 10 items of 114 documents
Albumin binding and hydrophobic character of promazine and chlorpromazine metabolites.
1972
1. The binding of didesmethylpromazine, promazine N-oxide, 2-hydroxypromazine, promazine sulfoxide, monodesmethylpromazine sulfoxide, didesmethylchlorpromazine, chlorpromazine N-oxide, and chlorpromazine sulfoxide to bovine serum albumin was determined by means of sephadex gel filtration. 2. The albumin binding of these substances was characterized by the following parameters: the percentage α of free substance, the percentage β of bound substance, the binding constants K1, k+ and m, the number of binding sites per albumin molecule, and the free binding energy ΔFo. 3. The partition coefficients between n-octanol and buffer solution, pH 7.40, were measured for the above mentioned metabolites…
Cationized albumin-biocoatings for the immobilization of lipid vesicles
2010
Tethered lipid membranes or immobilized lipid vesicles are frequently used as biomimetic systems. In this article, the authors presented a suitable method for efficient immobilization of lipid vesicles onto a broad range of surfaces, enabling analysis by quantitative methods even under rigid, mechanical conditions-bare surfaces such as hydrophilic glass surfaces as well as hydrophobic polymer slides or metal surfaces such as gold. The immobilization of vesicles was based on the electrostatic interaction of zwitterionic or negatively charged lipid vesicles with two types of cationic chemically modified bovine serum albumin (cBSA) blood plasma proteins (cBSA-113 and cBSA-147). Quantitative an…
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.
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…
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…
Inducing mixing of water-in water BSA/dextran emulsion by a strong polyelectrolyte
2015
Abstract We examine whether a small amount of strong polyelectrolyte (dextran sulfate sodium salt/DSS/) can induce mixing in water-in-water bovine serum albumin/dextran (BSA/DEX) emulsion and how intermacromolecular interactions affect its the rheological properties. Addition of DSS to water-in-water emulsion at pH 5.4 leads to its mixing at the DSS/BSA weight ratio, ( q ( DSS / BSA ) ) ≥ 0.07 , a noticeable increase in viscosity and storage modulus (G′). Mixing is reversible: increasing the ionic strength leads to phase separation in the water/BSA/DEX/DSS system. The increase in viscoelasticity results from the interaction of DSS with both macromolecular compounds of the emulsion. We assum…
Evaluation of the proteolysis degree with the o-phthalaldehyde/N-acetyl-L-cysteine reagent
1990
The o-phthalaldehyde/N-acetyl-L-cysteine (OPA-NAC) reagent is applied to the spectrophotometric evaluation of the proteolytic activity of enzymes. The high stability of the OPA-NAC isoindoles makes a strict control of the time of reaction unnecessary. A mathematical expression is proposed to calculate proteolysis degrees, where the absorbance decrease of the OPA-NAC derivative of the protein itself during the hydrolysis process is taken into account. The method is applied to bovine serum albumine, caseine, lysozyme, lactoglobuline and protamine sulphate as substrates, and pronase, papaine, trypsin and chymotrypsin as enzymes.
Irreversible formation of intermediate BSA oligomers requires and induces conformational changes.
2004
Understanding the relation between protein conformational changes and aggregation, and the physical mechanisms leading to such processes, is of primary importance, due to its direct relation to a vast class of severe pathologies. Growing evidence also suggests that oligomeric intermediates, which may occur early in the aggregation pathway, can be themselves pathogenic. The possible cytotoxicity of oligomers of non-disease-associated proteins adds generality to such suggestion and to the interest of studies of oligomer formation. Here we study the early stages of aggregation of Bovine Serum Albumin (BSA), a non pathogenic protein which has proved to be a useful model system. Dynamic light sc…