scholarly journals Molecular imprinting of bovine serum albumin and lysozyme within the matrix of polyampholyte hydrogels based on acrylamide, sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid and (3-acrylamidopropyl)trimethyl ammonium chloride

2021 ◽  
pp. 4-11
Author(s):  
Alexey Shakhvorostov ◽  
Sarkyt Kudaibergenov
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ammonium Chloride ◽  
Sodium Salt ◽  
Bovine Serum ◽  
In Situ Polymerization ◽  
Trimethyl Ammonium Chloride ◽  
Cationic Monomer ◽  
The Matrix ◽  
Adsorption Desorption

Molecularly-imprinted polyampholyte (MIP) hydrogels based on nonionic monomer – acrylamide (AAm), anionic monomer – sodium salt of 2-acrylamido-2-methyl-1-propanesulfonic acid (AMPS) and cationic monomer – (3-acrylamidopropyl)trimethyl ammonium chloride (APTAC) were obtained by immobilization of bovine serum albumin (BSA) and lysozyme in situ polymerization conditions. It was found that the best amphoteric hydrogel for sorption of BSA is APTAC-75H while for sorption of lysozyme is AMPS-75H. The sorption capacity of APTAC-75H and AMPS-75H with respect to BSA and lysozyme is 305.7 and 64.1-74.8 mg per 1 g of hydrogel respectively. Desorption of BSA and lysozyme from MIP template performed by aqueous solution of 1M NaCl is equal to 82-88%. Separation of BSA and lysozyme from their mixture was performed on MIP templates. The results of adsorption-desorption cycles of BSA on adjusted to BSA polyampholyte hydrogel APTAC-75H and of lysozyme on adjusted to lysozyme polyampholyte hydrogel AMPS-75H show that the mixture of BSA and lysozyme can be selectively separated with the help of MIP hydrogels.

scholarly journals Polycomplexes of Bovine Serum Albumin with Poly[2-Methacryloyloxy) Ethyl]Trimethyl Ammonium Chloride

2017 ◽  
Vol 4 (3) ◽  
pp. 195 ◽  
Author(s):  
Vitaliy V. Khutoryanskiy ◽  
Zauresh S. Nurkeeva ◽  
Grigoriy A. Mun ◽  
Natalie L. Rebenchuk ◽  
Anatoliy T. Ivaschenko ◽  
...  
Keyword(s):  
Ionic Strength ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Ammonium Chloride ◽  
Bovine Serum ◽  
Electrostatic Interactions ◽  
Ph Value ◽  
Solution Concentration ◽  
Water Soluble ◽  
Trimethyl Ammonium Chloride

Complex formation between bovine serum albumin and water-soluble synthetic cationic polyelectrolyte poly[2-methacryloyloxy)ethyl]trimethyl ammonium chloride has been studied in aqueous solutions by turbidimetric and viscometric methods. It was found that the structure of polycomplex is compact and its stability strongly depends on the environment. Formation of insoluble polycomplexes is observed in solutions with low ionic strength and pH, higher than 5.0. This pH value corresponds to the isoelectric point of the protein, so at lower pH the biopolymer macromolecules gain the positive charge and not able to be bound by the positively charged macromolecules of poly[2-methacryloyloxy)ethyl]trimethyl ammonium chloride. An increase of pH within 5.0-11.0 leads to further stabilization of polycomplex because of appearance of additional negative charges on biomacromolecules, caused by ionization of acidic groups. It was found that the main forces, which are responsible for the complexation, are electrostatic interactions.<br />The intensity of the complexation is dependent on the solution concentration, pH and ionic strength. In solutions with high ionic strength (I=0.2, 1.0) the mixing of the reagents does not lead to the formation of insoluble polycomplexes. The observed dependence is connected with the screening of electrostatic interactions between macromolecules of the biopolymer and synthetic polyelectrolyte by small ions present in solution.

The adsorption–desorption process of bovine serum albumin on carbon nanotubes

2007 ◽  
Vol 307 (2) ◽  
pp. 349-356 ◽  
Author(s):  
Laura E. Valenti ◽  
Pablo A. Fiorito ◽  
Carlos D. García ◽  
Carla E. Giacomelli
Keyword(s):  
Carbon Nanotubes ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Desorption Process ◽  
Adsorption Desorption

Relative stabilities of purified human mitochondrial and cytoplasmic isoenzymes of aspartate aminotransferase in lyophilized materials.

1979 ◽  
Vol 25 (5) ◽  
pp. 659-664 ◽  
Author(s):  
E J Sampson ◽  
S S McKneally ◽  
V S Whitner ◽  
C A Burtis ◽  
D D Bayse
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Aspartate Aminotransferase ◽  
Bovine Serum ◽  
Degradation Process ◽  
Storage Conditions ◽  
Apparent Difference ◽  
Reaction Solution ◽  
The Matrix ◽  
The Stability

Abstract Eight different pools of purified human mitochondrial and cytoplasmic isoenzymes of aspartate aminotransferase were prepared, to examine the effects of the following matrix variables: the matrix support material (bovine serum albumin and polyvinylpyrrolidone), endogenous pyridoxal concentration, and azide as an antimicrobial preservation. Storage temperatures of 25 and 37 degrees C were used as a rapid and convenient means of accelerating the degradation process. Activity of the enzyme was measured with and without pyridoxal in the reaction solution. We found that the mitochondrial isoenzyme was consistently more labile than the cytoplasmic isoenzyme under identical storage conditions. Both isoenzymes were more stable in matrixes containing bovine serum albumin than in those containing polyvinylpyrrolidone. No apparent difference in the stability of either isoenzyme was observed at matrix pyridoxal concentrations of 15 micromol/L and 150 micromol/L. Only the mitochondrial isoenzyme in matrixes containing bovine serum albumin and 15 micromol of pyridoxal per liter had increased activity (about 9%) when pyridoxal was added to the enzymatic reagent. The amount of activity in reconstituted specimens did not apparently change after 72 h at 4 degrees C.

scholarly journals Peculiarities of thermal aggregation of bovine serum albumin in the presence of strong polyelectrolytes

2020 ◽  
Vol 63 (9) ◽  
pp. 35-42
Author(s):  
Natalia N. Smirnova ◽  
◽  
Kirill V. Smirnov ◽  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Polymer Electrolyte ◽  
Sodium Salt ◽  
Bovine Serum ◽  
Temperature Increase ◽  
Hydrophobic Interactions ◽  
Maximum Yield ◽  
Maximum Output ◽  
Protein Molecules

The influence of temperature on bovine serum albumin (BSA) aggregation in aqueous solutions in the presence of poly-N,N-dimethyl-N,N-diallylammonium chloride (PDMDAAC) and the sodium salt of carboxymethylcellulose (CMC) was studied. It was shown that protein-polyelectrolyte complexes (PPC) form because of macromolecular reactions that are stabilized mainly by electrostatic forces. To characterize the PPC composition the φ parameter was used. This parameter is defined as the ratio of the concentration of ionic groups of polyelectrolyte per protein molecules. It was studied that when in an interpolyelectrolyte reaction, a sufficiently high degree of transformation occurs the polymer electrolyte initiates aggregation of protein molecules. As the temperature increases, the initiating role of the polymer electrolyte increases due to an increase in the intensity of hydrophobic interactions. Using the method of spectrophotometry, it was found that, depending on the nature of the polymer electrolyte, insoluble complexes of bovine serum albumin are formed when the pH parameter is above or below the isoelectric point of the protein, when its macromolecules are negatively or positively charged. In the presence of poly-N,N-dimethyl-N,N-diallylammonium chloride, the intensive formation of aggregates and their rapid precipitation in the form of flakes at pH > 7.0 was observed when the temperature increased to 60 °C. The maximum yield of the product of the interpolyelectrolyte reaction bovine serum albumin – sodium salt of carboxymethylcellulose was detected at pH ≤ 4.0. A temperature increase up to 60 °C, in this case, was not accompanied by intensive flocculation. Under optimal composition and interaction conditions, the degree of transformation in the BSA – PDMDAAX and BSA – CMC reactions is ~0.93 and 0.9, respectively, and decreases by ~5-7% with an increase in temperature to 60 °C. It was shown that for the same BOD composition (the ratio of components in the [CMC]/[BSA] complex = 0.1 g/g), an increase in temperature from 25 to 60 °C leads to the formation of particles that increase in size from 1 mcm to 5 mcm. The temperature increase leads to a change in composition of BOD, corresponding to its maximum output as a interpolyelectrolyte reactions product: for complex with PDMDAAC at T = 25, 40 and 60 °C, the φ value is 70, 60, 15; for the complex with the CMC – 60, 50, 20.

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