Use of liquid crystal to study the interactions of alkyl polyglycosides with gelatin and bovine serum albumin

2016 ◽  
Vol 27 (6) ◽  
pp. 852-856 ◽  
Author(s):  
Zhi-Jian Liao ◽  
Si-Nan Du ◽  
Yang Luo ◽  
Fang Zuo ◽  
Jian-Bin Luo
Keyword(s):  
Liquid Crystal ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Alkyl Polyglycosides

scholarly journals Bovine Serum Albumin Protein-Based Liquid Crystal Biosensors for Optical Detection of Toxic Heavy Metals in Water

Sensors ◽  
2020 ◽  
Vol 20 (1) ◽  
pp. 298 ◽  
Author(s):  
Noor ul Amin ◽  
Humaira Masood Siddiqi ◽  
Yang Kun Lin ◽  
Zakir Hussain ◽  
Nasir Majeed
Keyword(s):  
Heavy Metal ◽  
Liquid Crystal ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Metal Ions ◽  
Bovine Serum ◽  
Heavy Metal Ions ◽  
Limit Of Detection ◽  
Optical Image ◽  
Toxic Heavy Metals

A new methodology involving the use of Bovine Serum Albumin (BSA) as a probe and liquid crystal (LC) as a signal reporter for the detection of heavy metal ions in water at neutral pH was developed. BSA acted as a multi-dentate ligand for the detection of multiple metal ions. The LC sensor was fabricated by immobilizing 3 µg mL−1 BSA solution on dimethyloctadecyl-[3-(trimethoxysilyl)propyl]ammonium chloride (DMOAP)-coated glass slides. In the absence of heavy metal ions, a dark optical image was observed, while in their presence, a dark optical image turned to bright. The optical response was characterized by using a polarized optical microscope (POM). The BSA based LC sensor selectively detected toxic metal ions as compared to s block metal ions and ammonium ions in water. Moreover, the limit of detection was found to be very low (i.e., 1 nM) for the developed new biosensor in comparison to reported biosensors.

scholarly journals Highly sensitive bovine serum albumin biosensor based on liquid crystal

2014 ◽  
Vol 104 (4) ◽  
pp. 043705 ◽  
Author(s):  
Vikash Sharma ◽  
Ajay Kumar ◽  
Prasun Ganguly ◽  
A. M. Biradar
Keyword(s):  
Liquid Crystal ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Highly Sensitive

Detecting trypsin at liquid crystal/aqueous interface by using surface-immobilized bovine serum albumin

2016 ◽  
Vol 78 ◽  
pp. 213-220 ◽  
Author(s):  
Cheng-Hao Chuang ◽  
Yi-Cheng Lin ◽  
Wei-Long Chen ◽  
Yu-Hsuan Chen ◽  
Yu-Xun Chen ◽  
...  
Keyword(s):  
Liquid Crystal ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum

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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