The total serum protein concentration (C) was calculated as follows: C (mg/dl) = A sample × concentration of the standard A standard. 184.108.40.206 Albumin Serum albumin was determined using Bromocresol Green (BCG) method (Peter et al 1982). Measurement of serum albumin is based on its quantitative binding to the indicator 5, 5-dicromo-o-cresolsulphonaphthaline (bromocresol green, BCG). Non-haemoloysed serum was mixed with a buffered BCG reagent and incubated at 20-25oC for 5minutes. The absorbance of the sample and that of the standard were measured against the reagent blank at a wavelength of 630nm and albumin was calculated as follows: g/l = Δ A sample / Δ A standard × standard concentration (6%) (Where A = absorbance).
Given that mass was lost from the copper carbonate hydrate during heating, in this decomposition reaction, how many moles of solid product were produced? The molecular weight of the solid product is 79.545 g/mol (moles = mass / molecular weight). There were 4.183 x 10^-20 of solid product produced 4. Copper carbonate hydrate produces 1 mole of water (MW = 18.015 g/mol) was for every mole of solid product (MW = 79.545 g/mol) produced. Given that 3.327 g of product was produced during the reaction, how many grams of water were released as water vapor?
Primers used were supplied from Metabion (Germany) are listed in table (1). PCR amplification. Primers were utilized in a 25- µl reaction containing 12.5 µl of Emerald Amp Max PCR Master Mix (Takara, Japan), 1 µl of each primer of 20 pmol concentrations, 4.5 µl of water, and 6 µl of DNA template. The reaction was performed in an applied biosystem 2720 thermal cycler. 3.
Standard Preparation: 100 mg of standard ascorbic acid was weighed precisely and transferred to a 100 ml volumetric flask, added 70 ml of 0.5% sodium metabisulphite and dissolved by shaking. The volume was made up to the mark with 0.5% sodium metabisulphite for getting a concentration of 1 mg/ml. 2 ml of this solution was taken into another 100 ml volumetric flask and made the volume up to the mark with 0.5% sodium metabisulphite which resulted in concentration of 0.02 mg/ml. The solution was filtered through 0.45 µ nylon syringe filter. Sample Preparation: 2.5 g of sample was weighed accurately and transferred to a 100 ml volumetric flask.
The analysis was carried on C18 shim- pack GIST (150mmx 4.6mm 5µ) column used as stationary phase. A freshly prepared mobile phase consisting of methanol: potassium dihydrogen phosphate buffer in ratio of (30:70 v/v), PH-3 adjusted using ortho phosphoric acid (OPA) these were filtered by 0.45µM Whatmann filter paper and sonicated before use. The flow rate of mobile phase was 1ml/min. The detection was carried out at 220 nm and run time was around 10 minutes. Selection of wavelength A UV spectrum of drotaverine hydrochloride, ethamsylate, tranexamic acid in water was noted by scanning the solution in the range of 200-400nm.
(2004) with some modifications. Briefly, 10 µL of liver homogenate were mixed with 90 µL of low melting point agarose (0.7% in PBS) at 37 ºC and loaded on a fully frosted slide coated with 110 µl of normal melting point agarose (1% in PBS). Then this slide was coverslipped and the agarose layer was left 10 min at 4 °C to solidify. The cover slip was removed and the previous step was repeated for 5 min at 4 ºC. The slides were placed for 2 hrs at 4 °C in a lysis buffer containing (2.5 mol/L NaCl, 100 mmol/L Na2EDTA, 10 mmol/L Tris, [pH 10] and a freshly prepared 1% Triton X-100 and 10% Dimethyl sulfoxide were added to the buffer just before use).
In this experiment, racemic 2-methylcyclohexanone was reduced using sodium borohydride as a nucleophile to give a diastereomeric mixture of cis and trans secondary alcohols. The products were analyzed for purity using IR spectroscopy and gas chromatography. 1.2 g of 2-methylcyclohexanone and 10 mL of methanol were combined in a flask and cooled in an ice bath. Two 100 mg portions of sodium borohydride were added to the flask and stirred. 5 mL of 3M sodium hydroxide, 5 mL of de-ionized water, and 15 mL of hexane were added to the reaction flask and stirred.
Isolation of Ibuprofen: Fifteen 200 mg ibuprofen tablets were used, which was 3.37g (16.34 mmol, 112.3%) ibuprofen. This amount of ibuprofen was submerged in 25 mL of acetone and stirred vigorously for 5 minutes to dissolve. Red coatings of the tablet were separated and vacuum filtration was utilized to dissolve all insoluble components. The melting point range of the crude ibuprofen was 72.4-73.9°C. The major bands from the IR are, FTIR: sp3 O-H stretch, about 3200-2500 cm-1 (b, m); sp3 C-H stretch, 2991-2868 cm-1 (sh, m); sp2 =C-H stretch, 3100-3000 cm-1 (sh, w); sp2 C=O stretch, 1701 cm-1 (sh, s); and sp2-sp2, aromatic, C=C stretch (in ring), 1507 cm-1 (s, m).
To start an experiment of adsorption isotherm, Cu(II) aqueous solution of 100 ml with the predetermined varying initial concentration of Cu(II) in the range of 6.5-370.5 mg/l and the best activator composition of NaOH was put into the erlenmeyer flask and stirred using a magnetic stirrer at 75 rpm, room temperature of 298.15 K (± 2 K), 1 atm and normal pH. The experiment was stopped at 119 mins contact time for sampling. The samples of 1 ml were placed in a 20-ml vial and diluted with 10 ml distilled water, and filtered using a syringe filter. The filtrate was placed in 10-ml vial for the AAS analysis. To determine the concentration Cu(II) in the samples from the AAS reading, dilution factor was taken into
Approximately 1µg Mbgl was used with 5 mM 4-nitropheny-β-D-glucopyranoside (PNPG) in the reaction mixture of either 2 ml or 1 ml. The reaction was stopped by adding an equal volume of 0.2M Na2CO3and the released product 4-nitrophenol was quantified based on the millimolar extinction coefficient of 18.1 mM-1cm-1at 400 nm (Workman and Day 1982). The optimum pH was determined using the same assay in the 100 mM phosphate-citrate buffer in the pH range of 3.0 to 7.0 and for pH 8.0; 100 mMtris buffer was used. Similarly, the temperature optimum was determined in 100mM citrate buffer of pH-6.0. Thermal stability was determined by incubating the protein solution at 50°C and 55°Cfor different times followed by standard PNPG assay, as described earlier.