Investigation on Poly(methacrylic acid)-Grafted Cellulose/Bentonite Superabsorbent Composite: Synthesis, Characterization, and Adsorption Characteristics of Bovine Serum Albumin

2011 ◽  
Vol 50 (4) ◽  
pp. 1866-1874 ◽  
Author(s):  
T.S. Anirudhan ◽  
A. R. Tharun ◽  
S. R. Rejeena
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Methacrylic Acid ◽  
Bovine Serum ◽  
Adsorption Characteristics ◽  
Superabsorbent Composite ◽  
Composite Synthesis

Adsorption of Bovine Serum Albumin on Template-Polymerized Chitosan/Poly(methacrylic acid) Complexes

Langmuir ◽  
2007 ◽  
Vol 23 (14) ◽  
pp. 7687-7694 ◽  
Author(s):  
C. L. de Vasconcelos ◽  
P. M. Bezerril ◽  
T. N. C. Dantas ◽  
M. R. Pereira ◽  
J. L. C. Fonseca
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Methacrylic Acid ◽  
Bovine Serum

Temperature- and pH-responsive poly(N-isopropylacrylamide-co-methacrylic acid) microgels as a carrier for controlled protein adsorption and release

Soft Matter ◽  
2021 ◽  
Author(s):  
Priyanshi Agnihotri ◽  
Sangeeta Jangra ◽  
Shikha Aery ◽  
Abhijit Dan
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Adsorption ◽  
Methacrylic Acid ◽  
Bovine Serum ◽  
Ph Responsive ◽  
Ph Values ◽  
Different Temperatures ◽  
Adsorption And Release

Herein, we report controlled protein adsorption and delivery of thermo- and pH-responsive poly(N-isopropylacrylamide-co-methacrylic acid) (PNIPAM-co-MAA) microgels at different temperatures, pH values and ionic strengths by employing bovine serum albumin (BSA)...

Adsorption characteristics of bovine serum albumin onto alumina with a specific crystalline structure

2013 ◽  
Vol 25 (2) ◽  
pp. 453-459 ◽  
Author(s):  
Masakazu Kawashita ◽  
Junpei Hayashi ◽  
Zhixia Li ◽  
Toshiki Miyazaki ◽  
Masami Hashimoto ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Crystalline Structure ◽  
Bovine Serum ◽  
Adsorption Characteristics

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.

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