Sheet-like and tubular aggregates of protein nanofibril–phosphate hybrids

2019 ◽  
Vol 55 (3) ◽  
pp. 393-396 ◽  
Author(s):  
Xiangsheng Han ◽  
Lili Lv ◽  
Mingjie Li ◽  
Jun You ◽  
Xiaochen Wu ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Tubular Aggregates ◽  
Heating And Cooling

Nanofibrils assembled by bovine serum albumin aligned into microtubes and nanosheets upon heating and cooling its solution in phosphate buffer.

Bioceramic Hydroxyapatite Granules for Purification of Biotechnological Products

2011 ◽  
Vol 284-286 ◽  
pp. 1764-1769 ◽  
Author(s):  
Vitalijs Lakevics ◽  
Janis Locs ◽  
Dagnija Loca ◽  
Valentina Stepanova ◽  
Liga Berzina-Cimdina ◽  
...  
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Phosphate Buffer Solution ◽  
Sorption Process ◽  
Buffer Solution ◽  
Ph Values ◽  
Bovine Serum Albumin Adsorption ◽  
Albumin Adsorption

Sorption experiments of bovine serum albumin (BSA) on hydroxyapatite (HAp) ceramic granules, prepared at three temperatures 900°C, 1000°C and 1150°C were performed at room temperature 18,6 °C and phosphate buffer, pH 5,83; 6.38 and 7,39. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HAp ceramics specific surface area and pH values of phosphate buffer solution. However, it was confirmed that granule size was also an important parameter for bovine serum albumin adsorption. As a result of these experiments, the most appropriate adsorption conditions and phosphate buffer pH values influence on to BSA sorption were analyzed.

scholarly journals Electrochemical characterization and determination of carbamazepine as pharmaceutical standard and tablet content on gold electrode

2014 ◽  
Vol 68 (2) ◽  
pp. 207-212 ◽  
Author(s):  
Nemanja Trisovic ◽  
Bojan Bozic ◽  
Slobodan Petrovic ◽  
Svetlana Tadic ◽  
Milka Avramov-Ivic
Keyword(s):  
Cyclic Voltammetry ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Gold Electrode ◽  
Anticonvulsant Drug ◽  
Voltammetric Techniques ◽  
Anodic Behaviour

The anodic behaviour of carbamazepine (CBZ), an anticonvulsant drug, has been studied on gold electrode in 0.1 mol dm-3 phosphate buffer of pH 7.0 by using cyclic voltammetry. It has been found that the value of the oxidative current of pure CBZ at +0.90 V is a linear function of the concentration in a range from 1.0?10-7 to 1.0?10?4 mol dm?3. The detection of CBZ in the concentration of 1.0?10-8 mol dm-3 is among the lowest that have been reported for this drug using voltammetric techniques. CBZ as a content of tablet Galepsine? has been quantitatively determined. It has also been demonstrated that the modification of gold electrode with bovine serum albumin (BSA) results in a decrease of the oxidative peak current due to the binding of the drug to BSA.

BSA Adsorption on Hydroxyapatite after Thermal Treatment

2007 ◽  
Vol 361-363 ◽  
pp. 127-130 ◽  
Author(s):  
Elena Mavropoulos ◽  
Nilce C.C. da Rocha ◽  
Maria Helena M. Rocha-Leão ◽  
Antonella M. Rossi
Keyword(s):  
Thermal Treatment ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Active Sites ◽  
Sorption Process ◽  
Buffer Concentration ◽  
Surface Active ◽  
Bsa Adsorption

Adsorption experiments of bovine serum albumin on hydroxyapatite previously annealed at temperatures up to 1100°C was performed at 37°C and phosphate buffer, pH 6.0. Kinetic process was very efficient and irreversible for low phosphate buffer concentration. Thermal treatment contributed to the decrease of bovine serum albumin immobilization indicating that sorption process depended on HA specific surface area and the number of surface active sites. However, it was verified that particle size was also an important parameter for bovine serum albumin immobilization.

Influence of Blocking Agents on Non-Specific Background of Polystyrene Microbeads in Serum Immunoassay

2013 ◽  
Vol 641-642 ◽  
pp. 858-861 ◽  
Author(s):  
Zhi Min Ren ◽  
Xi Nie ◽  
Sheng Shu Ai
Keyword(s):  
Bovine Serum Albumin ◽  
Polyvinyl Alcohol ◽  
Serum Albumin ◽  
Human Serum ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Room Temperature ◽  
Tween 20 ◽  
Blocking Agents

In this paper, we used bovine serum albumin and polymer as the blocking agents and investigated the effect of blocking agents on non-specific background of polystyrene microbead that used the human serum immunoassay.The results showed that the nonspecific background is lower by using polymer blocking agents. The best blocking condition was that microbeads were blocked by PVXT (0.5% polyvinyl alcohol PVA, 0.8% polyvinylpyrrolidone, 0.05% Tween-20, PBS phosphate buffer, pH7.0) for two hours at room temperature.

Insights into the denaturation of bovine serum albumin with a thermo-responsive ionic liquid

Soft Matter ◽  
2014 ◽  
Vol 10 (33) ◽  
pp. 6161-6171 ◽  
Author(s):  
Wenlong Li ◽  
Peiyi Wu
Keyword(s):  
Phase Transition ◽  
Ionic Liquid ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Heating And Cooling ◽  
Dynamic Phase ◽  
Dynamic Phase Transition

The dynamic phase transition and denaturation mechanism of [P4,4,4,4][SS]–BSA–D2O solution during heating and cooling processes.

A radioimmunoassay for retinol-binding protein in serum and urine.

1985 ◽  
Vol 31 (8) ◽  
pp. 1364-1367 ◽  
Author(s):  
R Beetham ◽  
A Dawnay ◽  
J Landon ◽  
W R Cattell
Keyword(s):  
Polyethylene Glycol ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Binding Protein ◽  
Reference Interval ◽  
Retinol Binding Protein ◽  
Radial Immunodiffusion ◽  
Serum And Urine

Abstract In this radioimmunoassay for human retinol-binding protein (RBP), sample (serum, diluted as much as 3600-fold; or urine, diluted or undiluted) or calibrant (purified RBP in phosphate buffer containing bovine serum albumin) is incubated with 125I-labeled RBP and rabbit anti-human RBP antiserum for 24 h before separation with second antibody/polyethylene glycol. The assay's sensitivity is 5 micrograms/L, its useful working range 10 to 200 micrograms/L. The between-batch CV is 12.5% at 12 micrograms/L, 7% at 120 micrograms/L. Results correlate well (r = 0.99) with those by radial immunodiffusion. The reference interval for RBP in serum of men is 39-75 mg/L (mean 57), significantly (p less than 0.01) broader than for women (29-66 mg/L; mean 48). The 2.5-97.5 centile interval for RBP in urine is from less than 0.5 to 12.2 micrograms per millimole of creatinine (median 5.8). RBP in urine is unstable below pH 5.0 at 37 degrees C.

Assessment of corpus luteum function by direct radioimmunoassay for progesterone in blood spotted on filter paper.

1985 ◽  
Vol 31 (8) ◽  
pp. 1289-1293 ◽  
Author(s):  
P Petsos ◽  
W A Ratcliffe ◽  
D C Anderson
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Filter Paper ◽  
Phosphate Buffer ◽  
Bovine Serum ◽  
Solid Phase ◽  
Capillary Blood ◽  
Blood Spots ◽  
Multiple Sampling ◽  
Finger Prick

Abstract In this specific, direct RIA for progesterone in capillary blood dried on filter paper, progesterone is eluted, with phosphate buffer containing bovine serum albumin, from 5.9 microL of blood dried on 5.0-mm (diameter) discs of filter paper. The eluate is assayed, with 125I-labeled progesterone-11 alpha-glucuronyl-tyramine as tracer, with separation by a double-antibody solid-phase technique. The sensitivity of the assay is 4.7 pg per tube, corresponding to 2.5 nmol per liter of blood. Within- and between-batch CVs averaged 7.0 and 9.2%, respectively, over the working range of the assay (4.5-64 nmol/L). Concentrations of progesterone in blood spots (y) correlated well with those in serum (x) as measured by an established direct RIA (Clin Chem 28:1314, 1982): y = 0.430x - 2.44 (r = 0.972, n = 104). Progesterone is stable in the blood spots for at least 15 weeks at 25 degrees C. The convenience of multiple sampling of blood by finger prick and the simplicity of the assay make this approach useful in investigating serial progesterone concentrations in outpatients.

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.

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