scholarly journals Adsorption of bovine serum albumin on silver surfaces enhances the release of silver at pH neutral conditions

2015 ◽  
Vol 17 (28) ◽  
pp. 18524-18534 ◽  
Author(s):  
X. Wang ◽  
G. Herting ◽  
I. Odnevall Wallinder ◽  
E. Blomberg
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Surface Complexation ◽  
Surface Complexes ◽  
Silver Substrate ◽  
Neutral Conditions ◽  
Silver Surfaces

Enhanced release of silver in the presence of BSA due to surface complexation between BSA and the silver substrate, followed by exchange of surface complexes with BSA molecules in solution.

scholarly journals A simple method for non-denaturing purification of biotin-tagged proteins through competitive elution with free biotin

BioTechniques ◽  
2020 ◽  
Vol 68 (1) ◽  
pp. 41-44
Author(s):  
Kui Lin ◽  
Qin Yan ◽  
Audrey Mitchell ◽  
Natasha Funk ◽  
Catherlin Lu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Protein Purification ◽  
Recovery Rate ◽  
Bovine Serum ◽  
Protein Denaturation ◽  
Simple Method ◽  
Agarose Beads ◽  
Elution Buffer ◽  
Neutral Conditions

The use of avidin or streptavidin in the purification of biotinylated proteins has been highly restricted due to the harsh and denaturing elution conditions. Here, we use biotinylated bovine serum albumin as a working model to demonstrate a simple and rapid method for biotin-tagged protein purification under non-denaturing conditions. The biotinylated bovine serum albumin is specifically bound to the anti-biotin antibody agarose beads and competitively eluted with free biotin under near-neutral conditions. The optimized elution conditions include using 4 mg/ml biotin (pH 8.5) as the elution buffer and allowing the buffer to incubate with agarose beads for 30 min prior to elution. The elution recovery rate is over 85% without apparent protein denaturation. The method is applicable for both immunoprecipitation and column chromatography.

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.

Interaction of 1,4,7,10-Tetraazacyclododecane-Co(Ⅱ) with Bovine Serum Albumin

2013 ◽  
Vol 30 (2) ◽  
pp. 232
Author(s):  
Fan LIU ◽  
Yuanqin ZHANG ◽  
Zhijin ZHANG
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

Spectroscopic Studies on Interaction of Friedelin with Bovine Serum Albumin

2012 ◽  
Vol 18 (2) ◽  
pp. 287
Author(s):  
Zhiwei LIN ◽  
Zhengfu TAI ◽  
Zhongmin WAN ◽  
Fei WANG ◽  
Ningfei LEI
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Spectroscopic Studies
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