A Novel Approach to Magnetic Nanoadsorbents with High Binding Capacity for Bovine Serum Albumin

2007 ◽  
Vol 28 (3) ◽  
pp. 346-351 ◽  
Author(s):  
Yabin Sun ◽  
Xiaobin Ding ◽  
Zhaohui Zheng ◽  
Xu Cheng ◽  
Xinhua Hu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Capacity ◽  
High Binding ◽  
Novel Approach

scholarly journals Higher Cytokine and Opsonizing Antibody Production Induced by Bovine Serum Albumin (BSA)-Conjugated Tetrasaccharide Related to Streptococcus pneumoniae Type 3 Capsular Polysaccharide

2020 ◽  
Vol 11 ◽  
Author(s):  
Ekaterina A. Kurbatova ◽  
Nelli K. Akhmatova ◽  
Anton E. Zaytsev ◽  
Elina A. Akhmatova ◽  
Nadezhda B. Egorova ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Diagnostic Test ◽  
Bovine Serum ◽  
Capsular Polysaccharide ◽  
Binding Capacity ◽  
Immunological Study ◽  
Gm Csf ◽  
Test Systems ◽  
Type 3

A number of studies have demonstrated the limited efficacy of S. pneumoniae type 3 capsular polysaccharide (CP) in the 13-valent pneumococcal conjugate vaccine against serotype 3 invasive pneumococcal diseases and carriage. Synthetic oligosaccharides (OSs) may provide an alternative to CPs for development of novel conjugated pneumococcal vaccines and diagnostic test systems. A comparative immunological study of di–, tri–, and tetra–bovine serum albumin (BSA) conjugates was performed. All oligosaccharides conjugated with biotin and immobilized on streptavidin-coated plates stimulated production of IL-1α, IL-2, IL-4, IL-5, IL-10, IFNγ, IL-17A, and TNFα, but not IL-6 and GM-CSF in monocultured mice splenocytes. The tetrasaccharide–biotin conjugate stimulated the highest levels of IL-4, IL-5, IL-10, and IFNγ, which regulate expression of specific immunoglobulin isotypes. The tetra–BSA conjugate adjuvanted with aluminum hydroxide elicited high levels of IgM, IgG1, IgG2a, and IgG2b antibodies (Abs). Anti-CP-induced Abs could only be measured using the biotinylated tetrasaccharide. The tetrasaccharide ligand possessed the highest binding capacity for anti-OS and antibacterial IgG Abs in immune sera. Sera to the tetra–BSA conjugate promoted greater phagocytosis of bacteria by neutrophils and monocytes than the CRM197-CP-antisera. Sera of mice immunized with the tetra–BSA conjugate exhibited the highest titer of anti-CP IgG1 Abs compared with sera of mice inoculated with the same doses of di– and tri–BSA conjugates. Upon intraperitoneal challenge with lethal doses of S. pneumoniae type 3, the tri– and tetra–BSA conjugates protected mice more significantly than the di–BSA conjugate. Therefore, it may be concluded that the tetrasaccharide ligand is an optimal candidate for development of a semi-synthetic vaccine against S. pneumoniae type 3 and diagnostic test systems.

scholarly journals Increased binding and defective migration across fibronectin of cycling hematopoietic progenitor cells

Blood ◽  
2002 ◽  
Vol 99 (6) ◽  
pp. 2023-2031 ◽  
Author(s):  
Olivier Giet ◽  
Dirk R. Van Bockstaele ◽  
Ivano Di Stefano ◽  
Sandra Huygen ◽  
Roland Greimers ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Progenitor Cells ◽  
Bovine Serum ◽  
Binding Capacity ◽  
Hematopoietic Progenitor Cells ◽  
Hematopoietic Progenitor ◽  
Cd34 Cells ◽  
And Migration

Abstract Engraftment of hematopoietic progenitor cells has been shown to decrease during cell cycle transit. We studied cell cycle–associated changes in adhesion and migration of mitotically activated cord blood CD34+ cells. Migration toward medium conditioned by the stromal-derived factor-1–producing cell line MS-5 was studied in bovine serum albumin– and fibronectin (Fn)–coated transwells. Migration was reduced in cycling CD34+ cells and long-term culture-initiating cells (LTC-ICs) compared with their noncycling counterparts across Fn but not across bovine serum albumin. Conversely, Fn binding was higher in cycling CD34+ cells and LTC-ICs compared with noncycling progenitor cells, while adhesion of both subsets to bovine serum albumin was undetectable. The contribution of α4 and α5 integrins in mediating adhesion and migration of activated CD34+ cells onto Fn was analyzed by neutralization experiments. While α4-mediated Fn binding decreased during G2/M, α5 integrin–mediated adhesion increased during transit from G0/G1 to S and G2/M phases. As for migration, the contribution of α4 integrin was similar in all phases, whereas α5-directed migration was lower in G2/M compared with G0/G1and S phases. Defective migration of cycling CD34+ cells was not due to differences in α5 integrin expression. In conclusion, chemotaxis across Fn is less efficient in cycling progenitor cells in correlation with an increased Fn binding capacity. In addition, α4 and α5 integrin functions are independently modulated during cell cycle transit.

Effect of Denaturating Agents on the Structural Alterations and Drug-Binding Capacity of Human and Bovine Serum Albumin

2012 ◽  
Vol 45 (7) ◽  
pp. 520-529 ◽  
Author(s):  
J. Równicka-Zubik ◽  
A. Sułkowska ◽  
M. Maciążek-Jurczyk ◽  
L. Sułkowski ◽  
W. W. Sułkowski
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Binding Capacity ◽  
Drug Binding ◽  
Structural Alterations

Synthesis and Characterization of Hapten-Protein Conjugates for Antibody Production against Cyanogenic Glycosides

2015 ◽  
Vol 78 (7) ◽  
pp. 1408-1413 ◽  
Author(s):  
ISLAMIYAT FOLASHADE BOLARINWA
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Antibody Titer ◽  
Bovine Serum ◽  
Polyclonal Antibodies ◽  
Enzyme Linked Immunosorbent Assay ◽  
Cyanogenic Glycosides ◽  
Protein Conjugates ◽  
Novel Approach ◽  
Cyanogenic Plants

Consumption of cyanogenic plants can cause serious health problems for humans. The ability to detect and quantify cyanogenic glycosides, capable of generating cyanide, could contribute to prevention of cyanide poisoning from the consumption of improperly processed cyanogenic plants. Hapten-protein conjugates were synthesized with amygdalin and linamarin by using a novel approach. Polyclonal antibodies were generated by immunizing four New Zealand White rabbits with synthesized amygdalin-bovine serum albumin and linamarin-bovine serum albumin immunogen. This is the first time an antibody was produced against linamarin. Antibody titer curves were obtained from all the four rabbits by using a noncompetitive enzyme-linked immunosorbent assay. High antibody titer was obtained at dilutions greater than 1:50,000 from both immunogens. This new method is an important step forward in preventing ingestion of toxic cyanogenic glycosides.

Kainyl-bovine serum albumin: a novel ligand of the kainate subtype of glutamate receptor with a very high binding affinity

1989 ◽  
Vol 476 (1) ◽  
pp. 57-70 ◽  
Author(s):  
Nomi Eshhar ◽  
Gerardo Lederkremer ◽  
Michel Beaujean ◽  
Ora Goldberg ◽  
Paul Gregor ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Binding Affinity ◽  
Glutamate Receptor ◽  
Bovine Serum ◽  
High Binding ◽  
Very High ◽  
High Binding Affinity

scholarly journals The binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios

1974 ◽  
Vol 137 (3) ◽  
pp. 575-578 ◽  
Author(s):  
Geoffrey Allen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Sodium Dodecyl Sulphate ◽  
Bovine Serum ◽  
Equilibrium Dialysis ◽  
Sodium Dodecyl ◽  
Gel Filtration ◽  
Weight Ratio ◽  
Binding Ratio ◽  
High Binding

The extent of binding of sodium dodecyl sulphate to bovine serum albumin at high binding ratios was investigated by gel filtration. The weight ratio of bound sodium dodecyl sulphate to bovine serum albumin increases with the NaCl concentration, and, except at low salt concentrations, with the concentration of sodium dodecyl sulphate. In the presence of 1.0g of sodium dodecyl sulphate/l, the binding ratio varied from 1.0 (at 0.04m-Na+) to 2.2 (at 0.44m-Na+). In the presence of 0.24m-Na+, the binding ratio increased with sodium dodecyl sulphate concentration, from 0.9 (0.2g of sodium dodecyl sulphate/l) to 2.0 (5g of sodium dodecyl sulphate/l), at 26°C, in a dilute sodium phosphate buffer. No significant dependence of the binding ratio upon temperature in the range 26–45°C was observed. These results differ from those of Reynolds & Tanford (1970a) obtained by equilibrium dialysis.

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