ABSTRACT This study developed two adsorbents for extracting salbutamol sulphate (SAS) from water and urine samples after derivatisation with 2-aminobenzothiazole as a colour reagent. These adsorbents include cetylpyridinium chloride surfactant (CPC) modified silica and alumina-coated magnetite nanoparticles (Fe3O4/SiO2/CPC and Fe3O4/Al2O3/CPC). The derivatisation of SAS with the colour reagent resulted in an orange azo dye with maximum adsorption wavelengths of 443.0 nm. UV–Vis spectroscopy was used to identify the target analyte following the magnetic solid-phase extraction (MSPE) method. Under optimal conditions, the concentration ranges of 0.03–5.00 µg/mL and 0.05–6.00 µg/mL with good linearity (˃ 0.99), the detection limi

This study aims to deliver the woman’s image and to unveil on how to be introduced in the TV series. The research is based on the survey method-using content analysis tool. The research sample represented in the TV series produced by the IMN, which were displayed in 2014 and used the pattern of Margaret Gallagher to analyze the content of the series in accordance with the frame analysis theory.
The study came up with declination of the woman’s representation compared with man in Iraqi TV drama, also the study finds that the series introduced the woman according to the personal, social, political, and economic frames in a standardizing method. It focuses on the characteristics always attributed to it as showing her obedient of the

An easy, eclectic, precise high-Performance Liquid Chromatographic (HPLC) procedure was evolved and validated to estimate of Piroxicam and Codeine phosphate. Chromatographic demarcation was accomplished on a C₁₈ column [Use BDS Hypersil C₁₈, 5μ, 150 x 4.6 mm] using a mobile phase of methanol: phosphate buffer (60:40, v/v, pH=2.3), the flow rate was 1.1 mL/min, UV detection was at 214 nm. System Suitability tests (SSTs) are typically performed to assess the suitability and effectiveness of the entire chromatography system. The retention time for Piroxicam was found to be 3.95 minutes and 1.46 minutes for Codeine phosphate. The evolved method has been validated through precision, limit of quantitation, specificity,

Leucine amino peptidases (LAP; EC 3.4.11.1) constitute a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-terminal of protein or peptide substrates, (LAP) are present in animals, plants, and microbes. In this study, leucine amino peptidase was purified partial from Arachis hypogaea seeds by using gel filtration chromatography Sephadex G-100. The enzyme was purified 3.965 fold with a recovery of 29.4%. Its pH and temperature optimum were(8.7) and (37oC), respectively. The results show novel properties of LAP from Arachis hypogaea L. or peanut. The Km value for LAP (77 mM), with V max (1538 m mole min-1). We recommend a separate isoenzymeof the enzyme (LAP) from Arachis hypogaea on L. peanut seeds a

Beta-lactamase was purified from local isolate Klebsiella pneumonia by several steps included precipitation with ammonium sulphate at 20-40% saturation, DEAE- ion exchange chromatography and gel filtration on Sephacryl S-200 column. The obtained purification fold and recovery were 32.66; 47.04% respectively. The characterization of the purified beta-lactamase showed that the molecular weight was about 4000 daltons as determined by gel filtration.Purified enzyme had an optimal pH of 7 for activity and an optimal stability between pH 6.5-7.5, results shows that the optimal temperature appear to be 35 ? C .During storage the enzyme retained 72% at -20 ? C and retained 25% of the activity at the same period at 4 ? C.

Endoglucanase produced from Aspergillus flavus was purified by several steps including precipitation with 25 % ammonium sulphate followed by Ion –exchange chromatography, the obtained specific activity was 377.35 U/ mg protein, with a yield of 51.32 % .This step was followed by gel filtration chromatography (Sepharose -6B), when a value of specific activity was 400 U/ mg protein, with a yield of 48 %. Certain properties of this purified enzyme were investigated, the optimum pH of activity was 7 and the pH of its stability was 4.5, while the temperature stability was 40 °C for 60 min. The enzyme retained 100% of its original activity after incubation at 40 °C for 60 min; the optimum temperature for enzyme activity was 40 °C.