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

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.

2011 ◽  
Vol 284-286 ◽  
pp. 1764-1769 ◽  
Author(s):  
Vitalijs Lakevics ◽  
Janis Locs ◽  
Dagnija Loca ◽  
Valentina Stepanova ◽  
Liga Berzina-Cimdina ◽  
...  

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.


1995 ◽  
Vol 75 (4) ◽  
pp. 525-529 ◽  
Author(s):  
R. P. Del Vecchio ◽  
W. D. Sutherland ◽  
M. L. Connor

The purpose of this project was to develop a valid quantitative enzymeimmunoassay (EIA) for progesterone in blood plasma of cattle, pigs and sheep. Rabbit anti-progesterone, mouse monoclonal anti-rabbit IgG, authentic progesterone, and acetylcholine esterase bound covalently to progesterone were the principal reagents used to develop the EIA. Ninety-six well microliter plates were coated with mouse monoclonal anti-rabbit IgG and saturated with bovine serum albumin before use. Rabbit anti-progesterone was diluted to a working dilution of 1:2.0 × 106. Standard curves were linear and ranged from 1.56 to 400 pg of progesterone per well which allowed for the measurement of 0.03125 to 8.0 ng mL−1. Assay sensitivity averaged 1.56 pg well−1. Progesterone was extracted from plasma samples with petroleum ether. Plasma samples (n = 3 or 4 from each species) with unknown amounts of progesterone that were extracted and serially diluted with EIA buffer did not deviate from parallelism with progesterone standard curves in buffer. The correlation between EIA and radioimmunoassay (RIA) measurements of progesterone in the same plasma samples was high (P < 0.0001) for all three species (r = 0.96 for bovine; r = 0.96 for porcine; r = 0.94 for ovine). The regression of EIA data on RIA data produced the following equations:[Formula: see text]The intra- and inter-assay coefficients of variation were 5.4 and 10.6% for bovine, 5.8 and 11.0% for porcine and, 6.1 and 12.3% for ovine, respectively. These data show that this EIA is a valid and reliable memod for quantitating progesterone in extracts of bovine, porcine and ovine plasma. Key words: Enzymeimmunoassay, progesterone, plasma, bovine, porcine, ovine


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