Quantitative and Qualitative Evaluation of Adsorption/Desorption of Bovine Serum Albumin on Hydrophilic and Hydrophobic Surfaces

Langmuir ◽  
2009 ◽  
Vol 25 (19) ◽  
pp. 11614-11620 ◽  
Author(s):  
Y. L. Jeyachandran ◽  
E. Mielczarski ◽  
B. Rai ◽  
J. A. Mielczarski
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Qualitative Evaluation ◽  
Hydrophobic Surfaces ◽  
Adsorption Desorption ◽  
Hydrophilic And Hydrophobic Surfaces

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

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.

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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