Search results for "Serum albumin"
showing 10 items of 283 documents
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…
Enantioseparation of phenotiazines by affinity electrokinetic chromatography using human serum albumin as chiral selector
2007
Nowadays, there is a special interest within the pharmaceutical laboratories to develop single enantiomer formulations and consequently a need for analytical methods to determine the enantiomeric purity of drugs. The present paper deals with the enantiomeric separation of promethazine and trimeprazine enantiomers by affinity electrokinetic chromatography (AEKC)-partial filling technique using human serum albumin (HSA) as chiral selector. A multivariate optimization of the most critical experimental variables in enantioresolution, running pH, HSA concentration and plug length, is carried out to obtain enantioresolution of promethazine and trimeprazine. The estimated maximum and optimum resol…
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…
Role of Seroalbumin in the Cytotoxicity of cis-Dichloro Pt(II) Complexes with (N^N)-Donor Ligands Bearing Functionalized Tails
2018
Given the potent anticancer properties of cisdiamminedichloroplatinum( II) and knowing its mode of action, we synthesized four new cis-[PtCl2(N^N)] organoplatinum complexes, two with N-substituted pbi ligands (pbiR = 1-R-2-(2-pyridyl)benzimidazole) (namely, 1 and 2) and two more with 4,4′-disubstituted bpy ligands (bpy = 2,2′-bipyridine) (namely, 3 and 4). We explored their cytotoxicity and ability to bind to deoxyguanosine monophosphate (dGMP), DNA, and albumin models. By 1H NMR and UV−vis spectroscopies, circular dichroism, agarose gel electrophoresis, differential scanning calorimetry measurements, and density functional theory calculations, we verified that only 3 can form aquacomplex s…
Optical studies on interaction of biliary contrast agents with native and modified human serum albumin.
1981
The interaction of two homologous series of biliary contrast agents with native human and bovine serum albumin and with modified human serum albumin was investigated using circular dichroism and equilibrium dialysis. For most derivatives, extrinsic Cotton effects were observed for the interaction with both albumins. In some cases, these effects were strongly affected by only small changes in the chemical structure of the drugs. These large differences in extrinsic Cotton effects can be explained by definite effects of the chemical structures on the binding site selectivity of some drugs. For example, iopodate preferentially binds to the warfarin binding site of human Scrum albumin, while an…
The Interaction of Intravenous and Oral Biliary Contrast Agents with Serum Albumins
1978
The binding of two homologous series of oral and intravenous biliary contrast agents to human and bovine serum albumin was investigated using the gel filtration technique and circular dichroism measurements.