scholarly journals Protein-polyelectrolyte complexes. Part 3. Complexes bovine serum albumin with sulfonate-containing aromatic poly- and copolyamides

2019 ◽  
Vol 58 (4) ◽  
pp. 66-71
Author(s):  
Natalia N. Smirnova ◽  
◽  
Kirill V. Smirnov ◽  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Aromatic Polyamide ◽  
Density Maximum ◽  
Degree Of Ionization ◽  
Polyelectrolyte Complexes ◽  
Composition And Structure ◽  
Carboxylic Groups ◽  
Main Factor

The interaction of bovine serum albumin in aqueous solution with sulfonate-containing poly- and copolyamides were studied. It was shown that, as a result of macromolecular reactions protein-polyelectrolyte complexes forms, stabilized mainly by electrostatic forces. To characterize the protein-polyelectrolyte complexes composition the r parameter used, which is defines as the ratio of mass concentration of polyelectrolyte and protein. It was shown that the main factor determining the composition and structure of forming protein-polyelectrolyte complexes is the degree of ionization of functional groups, interacting in the polyelectrolyte reaction that is determined by the nature of those groups and the pH of the solution. The presen ce of sulfonate and carboxylic groups in the copolyamide composition gives an extra opportunity to regulate the protein-polyelectrolyte interactions. Using spectrophotometry were established that, in the studied system when the aromatic polyamide and bovine serum albumin are mixed at optimal pH conditions (рН < 4.9), complexes are formed, the composition of which corresponds to the value of r ~ 0.15 g/g. The degree of conversation in protein-polyelectrolyte reactions is close to 0.8. The size of the formed particles was about 2.2 μm. In the case of aromatic copolyamides that contain both sulfonate and carboxylic groups, an increase in concentration of carboxylic groups to 42 mol. % leads to a shift of the optical density maximum on the curve of turbidimetric titration in to the higher r values (~ 0.18 g/g) at pH = 3.5, when the carboxylic groups are non-ionized. The size of the formed complex particles was about ~ 150.0 nm, the fraction of micron-sized particles is about 5%. The degree of released protein is based on the conditions under which reaction take place and varies from 93 to 99%. The result obtained during this work can serve as a base for the effective methods of isolation and purifying of the target proteins development.

scholarly journals INTERACTION OF NATURAL AND SYNTHETIC POLYELECTROLYTES WITH BOVINE SERUM ALBUMIN

2019 ◽  
Vol 62 (7) ◽  
pp. 45-51
Author(s):  
Natalya N. Smirnova ◽  
Kirill V. Smirnov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Maximum Yield ◽  
Sodium Carboxymethylcellulose ◽  
Polyelectrolyte Complexes ◽  
Ionic Groups ◽  
Micron Size ◽  
Carboxylic Groups ◽  
Natural And Synthetic

Interaction of a number of natural and synthetic polyelectrolytes (PE): chitosan, poly‒N,N‒dimethyl‒N,N‒diallylammonium chloride, sodium carboxymethylcellulose and aromatic copolyamide, synthesized on the bases of dichloranhydride of isophthalic acid and two diamines (4,4’‒(2,2’‒sodium disulfonate)‒diaminodephenyl, 4,4’‒(2,2’‒dicarboxylic acid)‒diaminodiphenylmethyl) and bovine serum albumin (BSA) in aqueous solutions were studied. It was shown that as a result of macromolecular reactions protein‒polyelectrolyte complexes (PPC) forms, stabilized mainly by electrostatic forces. To characterize their composition we used the value of parameter φ, defined as an amount of ionic groups of polyelectrolytes calculated per macromolecule of protein. Using spectrophotometry and conductometry it was established that the composition of PPC in the studied systems when components are mixed at optimal conditions corresponds to the value of φ ~30 – 90. The conditions for the existence of insoluble PPC were determined. In the case of precipitation of poly-N,N‒dimethyl‒N,N‒diallylammonium chloride and chitosan in protein – polyelectrolyte reactions the maximum yield of the product is observed at pH ≥ 7. The introduction of sodium carboxymethylcellulose and aromatic copolyamide into the interaction with protein accompanied by shifting the range of PPC existence into the acidic region: the maximum yield of the product is observed at рН ≤ 4. The size of the formed complex particles ranges from 10 nm ([PE]/[BSA] = 0.01 – 0.05 g/g) to ~ 1.0 ‒ 5.5 μm ([PE]/[BSA] = 0.1 – 0.35 g/g). In case of relatively short‒chained aromatic copolyamide, containing significant amount of non‒ionized carboxylic groups, the ratio of micron size particles is about 5%. The presence of sulfonate and carboxylic groups in the composition of copolyamide gives an additional opportunity to regulate the conversation degree in the interpolyelectrolyte reactions, thus also implying the structure and the composition of the formed complexes.

scholarly journals Covalent Surface Functionalization of Bovine Serum Albumin to Magnesium Surface: Enhancing Robust Corrosion Inhibition and In vitro Osteo-Inductivity

2019 ◽  
Author(s):  
Seo Yeon Lee ◽  
Sita Shrestha ◽  
Bishnu K Shrestha ◽  
Chan Hee Park ◽  
Cheol Sang Kim
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Cost Effective ◽  
Corrosion Current ◽  
Covalent Modification ◽  
Carboxylic Groups ◽  
Bonding Method ◽  
Surface Modified

Herein, we describe precisely on covalent modification of pure magnesium (Mg) surface and applied to induce in vitro osteogenic differentiation. A new concept, chemical bonding method is proposed for developing stable chemical bonds on Mg surface through serial assembly of bioactive additives including ascorbic acid (AA) and bovine serum albumin (BSA). The coating with such potential materials shows strong integrity to the Mg and could suitable for cell-interface interaction with the host tissue during implantation in bone tissue repair. The physicochemical and electrochemical properties of surface modified Mg assess how these nanoscales layered of biomolecules could demonstrate the significance improvement in chemical stability of coating. The modified Mg-OH-AA-BSA exhibits better anti-corrosion behavior with high corrosion potential (Ecorr ~ ‒ 0.96 V) and low corrosion current density (Icorr ~ 0.2 &micro;A cm-2) as compared to pure Mg (Ecorr ~ ‒1.46 V, Icorr ~ 10.42 &micro;A cm-2). Outer layer of BSA on Mg protects fast degradation rate of Mg which is the consequence of strong chemicals bonds between amine groups on BSA with carboxylic groups on AA. Collectively, the results suggest that surface modified Mg provides strong bio-interface and enhances the proliferation and differentiation of pre-osteoblast (MC3T3-E1) cells through protein-lipid interaction. Owing to this fact, the cost-effective and scalable covalent functionalization of Mg surface inherits biological advantage in orthopedic and dental implants with long term stability.

scholarly journals Sorptive and Separation Properties of Ultrafiltration Membranes on the Basis of Sulfonate-Containing Polyamide with Respect to Bovine Serum Albumin

2012 ◽  
Vol 15 (1) ◽  
pp. 51
Author(s):  
N.N. Smirnova ◽  
Yu.A. Fedotov ◽  
I.A. Nebukina
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Hydrophobic Interactions ◽  
Sorption Isotherms ◽  
Aromatic Polyamide ◽  
Static Mode ◽  
Ionic Groups ◽  
Maximum Sorption ◽  
Membrane Protein Interaction

<p>Investigation of sorption of bovine serum albumin in the static mode and in ultrafiltration conditions by membranes produced from statistic copolymers of aromatic polyamides synthesized by polycondensation of the sodium salt of 4, 4/-diaminodiphenylamine-2-sulfo-acid and m-phenylenediamine in various ratios with chloroanhydride of isophthalic acid has been carried out. Interconnection has been established between the charge of protein macromolecules, concentration of fragments containing ionic groups in the aromatic polyamide and sorptive, separation and transport characteristics of membranes on its basis. It has been shown that dominant forces that determine membrane/protein interaction in the systems under consideration are coulomb forces, but the contribution of hydrophobic interactions is also significant. The results of mathematical processing of experimental data indicate that there is a good compliance of sorption isotherms with Langmuir’s model. Depending on the concentration of fragments containing ionic groups in the polyamide and pH of the solution, the calculated values of maximum sorption in sorbent/sorbate systems under consideration vary in the range of 0.028 to 0.338 mg/cm<sup>2</sup>. Dynamic investigations have shown that selectivity of the membranes is 85 to 98%. To assess the sorptive activity of the membranes in the course of ultrafiltration, indicators of sorption and sorptive losses calculated on the basis of the ratio of the change of mass content of protein in the process of filtration to the initial value have been used. Depending on the material used to produce the membrane and pH of the solution being filtered, sorptive losses range from 5 to 33%. Their minimum value is observed when pH is higher than the isoelectric point of the protein, i.e. in the field where protein macromolecules and the surface of the membrane have like charges.</p>

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.

Stability of Prostacyclin in Human Plasma and Whole Blood: Studies on the Protective Effect of Albumin

1981 ◽  
Vol 46 (03) ◽  
pp. 645-647 ◽  
Author(s):  
M A Orchard ◽  
C Robinson
Keyword(s):  
Platelet Aggregation ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protective Effect ◽  
Whole Blood ◽  
Bovine Serum ◽  
Fatty Acid Content ◽  
Krebs Solution ◽  
Antiaggregatory Activity ◽  
Free Plasma

SummaryThe biological half-life of prostacyclin in Krebs solution, human cell-free plasma or whole blood was measured by bracket assay on ADP-induced platelet aggregation. At 37°C, pH 7.4, plasma and blood reduced the rate of loss of antiaggregatory activity compared with Krebs solution. The protective effect of plasma was greater than that of whole blood. This effect could be partially mimicked by the addition of human or bovine serum albumin to the Krebs solution. The stabilisation afforded by human serum albumin was dependent on the fatty acid content of the albumin, although this was less important for bovine serum albumin.

RADIOIMMUNOASSAY OF OESTRONE AND OESTRADIOL IN THE PERIPHERAL PLASMA OF THE DOMESTIC FOWL IN VARIOUS PHYSIOLOGICAL STATES AND OF HYPOPHYSECTOMIZED AND OVARIECTOMIZED FOWLS

1974 ◽  
Vol 75 (1) ◽  
pp. 133-140 ◽  
Author(s):  
B. E. Senior
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diethyl Ether ◽  
Bovine Serum ◽  
Domestic Fowl ◽  
Laying Hens ◽  
Peripheral Plasma ◽  
The Mean ◽  
Precision And Accuracy ◽  
Chicken Ovary

ABSTRACT A radioimmunoassay was developed to measure the levels of oestrone and oestradiol in 0.5–1.0 ml of domestic fowl peripheral plasma. The oestrogens were extracted with diethyl ether, chromatographed on columns of Sephadex LH-20 and assayed with an antiserum prepared against oestradiol-17β-succinyl-bovine serum albumin using a 17 h incubation at 4°C. The specificity, sensitivity, precision and accuracy of the assays were satisfactory. Oestrogen concentrations were determined in the plasma of birds in various reproductive states. In laying hens the ranges of oestrone and oestradiol were 12–190 pg/ml and 29–327 pg/ml respectively. Levels in immature birds, in adult cockerels and in an ovariectomized hen were barely detectable. The mean concentrations of oestrone and oestradiol in the plasma of four non-laying hens (55 pg/ml and 72 pg/ml respectively) and one partially ovariectomized hen (71 pg/ml and 134 pg/ml respectively) were well within the range for laying hens. It is evident that the large, yolk-filled follicles are not the only source of oestrogens in the chicken ovary.

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