92% of the non-endodontists were not aware about the use of sodium hypochlorite as a bleaching agent and considered irrigation to be its only use. Liquid chlorine bleach, an alkaline solution of sodium hypochlorite is highly effective on white fabrics and provides germicidal activity as
The amino acid sequence of Ara h 7 is 53% similar to Ara h 6, while 35% similar to Ara h 2 , but are less stable than both due to conservation of only two disulphide bonding. Schmidt et al.,  enriched and separated peanut proteins of molecular weight less than 20 kDa on 2D gel electrophoresis. After mass spectroscopic analysis, two isoallergens were found one of which had an additional pro-peptide cleavage point. Furthermore, the putative cleavage point demonstrates the biological function of conglutins as an amylase/trypsin
Standardization of NaOH solution Accurately weigh out a sample of approximately 0.3-0.4 g of primary standard potassium hydrogen phthalate, KHPh, which has been previously dried at 120°C. Do not use more than 0.4 g. To obtain an accurate mass, weigh the sample on weighing paper, slide it into a clean (but not necessarily dry) 250 mL Erlenmeyer flask and reweigh the paper to account for any KHPh that may remain on it. Dissolve the KHPh sample in about 50 mL of CO2-free water and add 2-3 drops of 0.1% phenolphthalein indicator. Begin adding the approximately 0.1 M sodium hydroxide solution from the buret while continuously swirling the flask contents. Do not open the stopcock completely.
However, all proteins are constructed from the same set of 20 amino acids linked in unbranched polymers. The covalent bond that exists between amino acids is called peptide bond, hence a polymer of amino acids is named polypeptide. A protein is a biological functional molecule made up of one or more polypeptides which is folded and coiled into unique three-dimensional structure. In laboratory, it is important to measure the concentration of proteins for research investigations. Biuret test is adopted to quantify proteins in fluid by using a spectrophotometer.
The sample was transferred to a 250 ml conical flask kept in water bath for alkali treatment. 75 ml of 17.5% caustic soda was measured using a measuring cylinder at 20°C. 15 ml of 17.5% NaOH was added and fibres were macerated gently with a flattened glass rod for 1 minute. 10 ml more NaOH was added and the solution was mixed for 45 seconds. 10 ml NaOH was again added and mixed for 15 seconds to make lump free slurry.
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 .
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
The DEAE CL-6b gel was washed twice with 0.5m Hcl, twice with 0.5m Naoh and twice with PB ph6.0 before utilization. For DEAE 1ml gel every 1ml serum was utilized. In the wake of blending for 1 hour at 200c the suspension was centrifuged at 4500g for 25 minutes. The supernatant was thought by Ammonium sulfate precipitation and pellet was broken up in refined water and the ensuing arrangement was dialyzed against PBS ph7.2 to evacuate Ammonium sulfate and conformed to the first volume with yhe same cushion (Hong et.al., 1994). 2)
6 H2O) in 100 ml distilled water. (vi) 0.2(N) Sodium Hydroxide solution: Dissolve 8.0 gm sodium hydroxide in 1 l distilled water. (vii) Acetic acid: Dilute 1 part of glacial acid with 4 parts of water. (viii) Stock cyanide solution: Dissolve 2.51 gm potassium cyanide (A.R. Grade) in 1 l water, standardize this solution with 0.0192(N) silver nitrate solution.
In 1975, Yoshimura M, et al. isolation, and purification of Monascus pigments through column chromatography by using Sephadex G-50 (3 cm × 5 cm) column with 0.1 M potassium phosphate buffer of pH 7.0 was used as effluent for flow rate of 0.5 mL/min. A number of column and eluants were preferred to isolation and purification of different Monascus pigments by researchers. In 1983, Hin-Chung Wong and Philip E. Koehler used silica gel column, 2× 20 cm, 60- 200 mesh suspended in hexane