A total of 0.1 ml of supernatant was added to cuvette containing 1.9 ml of 50mM phosphate buffer (pH 7). The reaction was started by the addition of 1 ml freshly prepared 30mM H2O2. The rate of decomposition of H2O2 was measured spectrophotometrically at 240 nm. Catalase values were expressed as n moles H2O2 consumed/min/mg protein. Measurement of lipid peroxidation TBARS, a measure of lipid per oxidation, was measured as described by Ohkawa .
The reaction mixture contained 100 µl of each of the extract solution in separate tubes (1 mg/ml) to which was added 0.5 ml of Folin-Ciocalteu phenol reagent, 1.5 ml of 20% (w/v) sodium carbonate and 10 ml of distilled water. After 2h of reaction at ambient temperature, the absorbance was measured at 765 nm and used to calculate the phenolic contents, using gallic acid as a standard. All experiments were performed thrice and the results were averaged and reported in the form of mean ± S.D.Then the total phenolic contents were expressed in term of gallic acid equivalents (mg GAE/g dry extract)
[Figure 1] 2.2.1. Chloromethylation of poly sulphone 5 g of polysulphone was dissolved in 75 mL of chloroform at 70°C. After complete dissolution of polymer, a mixture of paraformaldehyde (3.4 g) and chlorotrimethylsilane (14.7) mL was prepared as the chloromethylating agent with constant stirring which was followed by the addition of 5% of stannous chloride (by weight, of polymer) as catalyst with stirring at 70°C and allowed to react for 18 h. Then the polymer was precipitated in methanol to eliminate
This solution was diluted with diluents to gae a concentration of 0.1 mg/ml solution each of Amoxicillin trihydrate. The HPLC method was applied to the solutions and the results obtained were shown in table 4.6.11. System suitability solution: 25.0 µg/mL each of of USP Amoxicillin RS in Diluent. Precision
Separations were performed on a chiral AGP (100mm×4.6mm id, 5µm particle size) column using UV detector at 301 nm. The mobile phase constituted of 0.025mol L-1 di sodium hydrogen phosphate and Acetonitrile, (90:10 v/v) (pH 7.0) and diluted onto ortho phosphoric acid was used for ph adjustment. An Inertsil ODS (4cm ×4.6mm i.d.) was used as guard column. A flow rate of 1.0 mL/min was maintained throughout the analysis.
Catalytic reduction of p-nitrophenol As a model reaction, we selected the reduction of 4-NP by NaBH4 to 4-AP. The reduction was followed with the aqueous solution in a standard quartz cell with a 1cm path length. The reaction process was as follows: 1.5 mL of 0.15 mM 4-NP was mixed with 1.0 mL of 0.02 M NaBH4 in the cell for UV-Vis measurements. Immediately, the colour change was observed from light yellow to deep yellow. 0.5 mL of AuNPs solution was added to the above mixture.
During the experiment, the solution in the receptor side was maintained at 370C and stirred at 800 rpm with Teflon coated magnetic stirrer bar. At fixed time intervals, 3ml of the sample was withdrawn from the receiver compartment through side tube and analyzed spectrophotometrically at 353 nm by the UV-VIS spectrophotometer. A graph of % cumulative drug release against time was plotted as depicted in Table 5.6 and shown in Fig 5.5
1. Preparation of oxidized starch Oxidized starch was prepared according to the method of Forssel et al. (1995) with slight modifications. 50% slurry of starch was prepared by dispersing 50g of starch in 100 ml of distilled water. The pH was adjusted to 9.5 with 2M NaOH.
The extract was centrifuged at 20,000 rpm for 10 minutes at 4°C, the clear supernatant being taken for enzyme assay. Assay Catalase was assayed at 37°C in a reaction mixture containing 1.9ml of 0.1M sodium phosphate buffer pH 7.0 in 0.1ml of enzyme extract. The reaction was initiated by adding 1ml of H2O2 to the reaction mixture. The rate of decrease in absorbance at 240 nm was measured at 10 second intervals for 1 min. The specific activity of CAT was expressed in terms of unit of H2O2 decomposed per min per mg of protein.