SEDIMENTATION AND VISCOSITY STUDIES OF BOVINE SERUM ALBUMIN IN UREA SOLUTION

1955 ◽  
Vol 33 (6) ◽  
pp. 1043-1054 ◽  
Author(s):  
P. A. Charlwood
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Axial Ratio ◽  
Protein Molecule ◽  
Mercury Compound ◽  
Urea Solution ◽  
Initial Increase ◽  
Viscosity Measurements

Sedimentation and viscosity measurements were made on bovine serum albumin during denaturation at pH 9.9 in 8.0 M urea in the presence of sodium-p-chloromercuribenzoate. The results suggested that the urea caused a rapid initial increase in the axial ratio and equivalent volume of the protein molecule. A subsequent slower increase in asymmetry was attributed to the effect of the mercury compound.

scholarly journals Ketoprofen-Based Ionic Liquids: Synthesis and Interactions with Bovine Serum Albumin

Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 90 ◽  
Author(s):  
Paula Ossowicz ◽  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Joanna Klebeko ◽  
Ewelina Świątek ◽  
...  
Keyword(s):  
Ionic Liquids ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Binding Mode ◽  
Pharmaceutical Ingredients ◽  
System A ◽  
Static Mechanism

The development of ionic liquids based on active pharmaceutical ingredients (API-ILs) is a possible solution to some of the problems of solid and/or hydrophobic drugs such as low solubility and bioavailability, polymorphism and an alternative route of administration could be suggested as compared to the classical drug. Here, we report for the first time the synthesis and detailed characterization of a series of ILs containing a cation amino acid esters and anion ketoprofen (KETO-ILs). The affinity and the binding mode of the KETO-ILs to bovine serum albumin (BSA) were assessed using fluorescence spectroscopy. All compounds bind in a distance not longer than 6.14 nm to the BSA fluorophores. The estimated binding constants (KA) are in order of 105 L mol−1, which is indicative of strong drug or IL-BSA interactions. With respect to the ketoprofen-BSA system, a stronger affinity of the ILs containing l-LeuOEt, l-ValOBu, and l-ValOEt cation towards BSA is clearly seen. Fourier transformed infrared spectroscopy experiments have shown that all studied compounds induced a rearrangement of the protein molecule upon binding, which is consistent with the suggested static mechanism of BSA fluorescence quenching and formation of complexes between BSA and the drugs. All tested compounds were safe for macrophages.

scholarly journals The dipolar origin of protein relaxation

1968 ◽  
Vol 110 (3) ◽  
pp. 419-424 ◽  
Author(s):  
H. Hendrickx ◽  
R. Verbruggen ◽  
M. Y. Rosseneu-Motreff ◽  
V. Blaton ◽  
H. Peeters
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Axial Ratio ◽  
Ion Exchange Resin ◽  
Dielectric Dispersion ◽  
Dipole Relaxation ◽  
Ellipsoid Of Revolution ◽  
Dielectric Increment ◽  
Protein Relaxation

1. A set of parameters is proposed to check the interpretation of the dielectric behaviour of protein solutions as a rigid-dipole relaxation of prolate ellipsoids of revolution in the frequency range between 20 kHz and 10 MHz. Besides the δb-function of Scheraga, another analogous function (δa) is presented to establish size and shape of globular proteins. A study of the influence of solvent viscosity on the dielectric dispersion also gives strong evidence in favour of rigid-dipole relaxation. 2. Measurements of the dielectric dispersion of monomer solutions of bovine serum albumin and transferrin are reported. Monomers of bovine serum albumin were obtained by fractionation on Sephadex G-150. Low-conductivity solutions of both proteins are obtained by passage through an ion-exchange resin. 3. Computer analysis of the experimental dispersion curves by use of a two-term Debye dispersion gives valuable information about transferrin and leads to an axial ratio 4·5 for a prolate ellipsoid of revolution. The dielectric increment of bovine serum albumin is very low and no conclusive results have yet been obtained.

A novel potentiometric sensor based on urease/ bovine serum albumin-poly(3,4-ethylenedioxythiophene)/Pt for urea detection

2016 ◽  
Vol 71 (4) ◽  
pp. 277-282 ◽  
Author(s):  
Chien-Hsing Hsu ◽  
Ya-Wei Hsu ◽  
Yu-Ching Weng
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
High Selectivity ◽  
Ph Value ◽  
Detection Sensitivity ◽  
Urea Solution ◽  
Pt Electrode ◽  
Amide Bonds ◽  
Order Of Magnitude

AbstractWe have presented a potentiometric urea sensor using an urease/bovine serum albumin (BSA)-poly(3,4-ethylenedioxythiophene)(PEDOT)/Pt electrode. A urea detection sensitivity of 15.2 mV/decade (order of magnitude) has been achieved. BSA trapped in the PEDOT matrix was employed to bond urease molecules on the surface of a BSA-PEDOT/Pt electrode via amide bonds formed between the carboxyl functional groups on the enzyme and the amines on the BSA. The effects of PEDOT thickness, pH value of the urea solution, urease concentration, and temperature on the urea detection sensitivity were also studied. The lifetime of the sensor was studied for a period of 10 weeks, and the average sensing degradation rate was about 9 % per week. This sensor displayed a high selectivity to urea over glucose, KCl, and NaCl.

scholarly journals Deuteroporphyrin-albumin binding equilibrium. The effects of porphyrin self-aggregation studied for the human and the bovine proteins

1985 ◽  
Vol 229 (1) ◽  
pp. 197-203 ◽  
Author(s):  
M Rotenberg ◽  
R Margalit
Keyword(s):  
Human Serum Albumin ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Bovine Serum ◽  
Binding Constants ◽  
Protein Molecule ◽  
Competitive Model ◽  
Phosphate Buffered Saline ◽  
Self Aggregation

The binding equilibrium of deuteroporphyrin IX to human serum albumin and to bovine serum albumin was studied, by monitoring protein-induced changes in the porphyrin fluorescence and taking into consideration the self-aggregation of the porphyrin. To have control over the latter, the range of porphyrin concentrations was chosen to maker dimers (non-covalent) the dominant aggregate. Each protein was found to have one high-affinity site for deuteroporphyrin IX monomers, the magnitudes of the equilibrium binding constants (25 degrees C, neutral pH, phosphate-buffered saline) being 4.5 (+/- 1.5) X 10(7) M-1 and 1.7 (+/- 0.2) X 10(6) M-1 for human serum albumin and for bovine serum albumin respectively. Deuteroporphyrin IX dimers were found to bind directly to the protein, each protein binding one dimer, with high affinity. Two models are proposed for the protein-binding of porphyrin monomers and dimers in a porphyrin system having both species: a competitive model, where each protein molecule has only one binding site, which can be occupied by either a monomer or a dimer; a non-competitive model, where each protein molecule has two binding sites, one for monomers and one for dimers. On testing the fit of the data to the models, an argument can be made to favour the non-competitive model, the equilibrium binding constants of the dimers, for the non-competitive model (25 degrees C, neutral pH, phosphate-buffered saline), being: 8.0 (+/- 1.8) X 10(8) M-1 and 1.2 (+/- 0.6) X 10(7) M-1 for human serum albumin and bovine serum albumin respectively.

Molecular Weight of Ovalbumin and of Bovine Serum Albumin in Urea Solution

Nature ◽  
1955 ◽  
Vol 176 (4485) ◽  
pp. 738-738 ◽  
Author(s):  
H. A. McKENZIE ◽  
M. B. SMITH ◽  
R. G. WAKE
Keyword(s):  
Molecular Weight ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Urea Solution

scholarly journals Investigation of bovine serum albumin aggregation upon exposure to silver(i) and copper(ii) metal ions using Zetasizer

2021 ◽  
Vol 19 (1) ◽  
pp. 987-997
Author(s):  
Hassan A. Alhazmi ◽  
Waquar Ahsan ◽  
Angum M. M. Ibrahim ◽  
Rawan Ali Yahya Khubrani ◽  
Zainab Ali Abdullah Haddadi ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Zeta Potential ◽  
Serum Albumin ◽  
Metal Ions ◽  
Binding Sites ◽  
Neurological Disorders ◽  
Bovine Serum ◽  
Protein Molecule ◽  
Protein Aggregate ◽  
Bsa Aggregation

Abstract Depending upon the metal coordination capacity and the binding sites of proteins, interaction between metal and proteins leads to a number of changes in the protein molecule which may include the change in conformation, unfolding, overall charge, and aggregation in some cases. In this study, Cu(ii) and Ag(i) metal ions were selected to investigate aggregation of bovine serum albumin (BSA) molecule upon interaction by measuring the size and charge of the aggregates using nano-Zetasizer instrument. Two concentrations of metal ions were made to interact with a specific concentration of BSA and the size and zeta potential of BSA aggregates were measured from 0 min upto 18 h. The Cu(ii) and Ag(i) metal ions showed almost similar behavior in inducing the BSA aggregation and the intensity of peak corresponding to the normal-sized protein decreased with time, whereas the peak corresponding to the protein aggregate increased. However, the effect on zeta potential of the aggregates was observed to be different with both metal ions. The aggregation of protein due to interaction of different metal ions is important to study as it gives insight to the pathogenesis of many neurological disorders and would result in developing effective ways to limit their exposure.

scholarly journals Study of Bovine Serum Albumin Solubility in Aqueous Solutions by Intrinsic Viscosity Measurements

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Martin Alberto Masuelli
Keyword(s):  
Aqueous Solution ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Intrinsic Viscosity ◽  
Conformational Changes ◽  
Bovine Serum ◽  
Experimental Measurements ◽  
Viscosity Measurements ◽  
The Relationship

The behavior of bovine serum albumin (BSA) in water is scarcely studied, and the thermodynamic properties arising from the experimental measurements have not been reported. Intrinsic viscosity measurements are very useful in assessing the interaction between the solute and solvent. This work discussed in a simple determination of the enthalpy of BSA in aqueous solution when the concentration ranges from 0.2 to 36.71% wt. and the temperature from 35 to 40°C. The relationship between the concentration and intrinsic viscosity is determined according to the method of Huggins. The temperature increase reduces the ratio between inherent viscosity and concentration (ηi/c). This is reflected in the Van't Hoff curve. Furthermore, this work proposes hydrodynamic cohesion value as an indicator of the degree of affinity of protein with water and thermodynamic implications in conformational changes.

Improvement of an artificial test substrate technique for evaluation of em immunocytochemical labeling

1987 ◽  
Vol 45 ◽  
pp. 762-763
Author(s):  
G. D. Gagne ◽  
M. F. Miller
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Artificial Substrate ◽  
Chemical Fixation ◽  
As If

We recently described an artificial substrate system which could be used to optimize labeling parameters in EM immunocytochemistry (ICC). The system utilizes blocks of glutaraldehyde polymerized bovine serum albumin (BSA) into which an antigen is incorporated by a soaking procedure. The resulting antigen impregnated blocks can then be fixed and embedded as if they are pieces of tissue and the effects of fixation, embedding and other parameters on the ability of incorporated antigen to be immunocyto-chemically labeled can then be assessed. In developing this system further, we discovered that the BSA substrate can also be dried and then sectioned for immunolabeling with or without prior chemical fixation and without exposing the antigen to embedding reagents. The effects of fixation and embedding protocols can thus be evaluated separately.

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