Thus a solution α-naphthol 1a‚ 4-methylbenzaldehyde 2a and tert-butyl isocyanide 3a in EtOH was magnetically stirred at 45 C for 12 hours under an oxygen atmosphere with an equimolar ratio of the three reactants. TLC monitoring of the reaction mixture exhibited formation of a new product‚ which was purified (Table 1‚ entry 1). Identification of its structure by NMR spectroscopy revealed that it was 2-(4-methylbenzoyl)-1-naphthyl N-(tert-butyl)carbamate (4a). Next‚ in order to improve the yield of
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In order to read DNA‚ it must be sequenced. This sequencing uses electrophoresis‚ a technique that separates sections of DNA that differ by a base. Electrophoresis used to be done manually‚ but was error prone and time consuming. Now‚ automatic sequencing machines are used. A technician begins the process by pouring gel between two glass plates that are set less than half a millimeter apart. After the gel is set up‚ DNA is put into each of the ninety-six lanes. The DNA sections then move through
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Based on the data from the riboflavin spectrum scan‚ the maximum absorbance wavelength for this compound is 446 nm. This was the point between 390 nm and 500 nm at which the absorbance value (0.72) was the highest. A blank tube that has the components of the solution being examined except for the compound of interest is then used in combination to provide an even more accurate reading. Then‚ by using Beer’s Law‚ the molar extinction coefficient for riboflavin was able to be calculated: 14‚400 L/(moles*cm)
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The characteristic properties of slime can be explained by polymerisation reactions. Polymers can be explained most simply by the polymerisation of the molecule ethylene into polyethylene (see figure 1 below). Figure 1. Polymerisation of polyethylene from ethylene. In this example‚ the double bond between the carbon atoms is broken‚ allowing each carbon atom to form one more bond between another molecule. The double bond between the carbon atoms is weaker because the type of orbital is ‚ compared
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The first step was to prepare 400 mL of an 0.1 M solution of NaOH. This was done by diluting from the 6 M solution that was provided. Next‚ 0.715g of KHP was weighed using the glazed paper and the triple beam balance. The KHP was then transferred to the 250 mL Erlenmeyer flask. Using a graduated cylinder‚ 50 mL of deionized water was measured and added to the flask. The KHP was dissolved in the water‚ and few drops of phenolphthalein were added. Moreover‚ the burette was rinsed with deionized water
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Specimen Preparation: Samples and all test reagent and kit were brought into room temperature. In 2ml eppendrof tube approximately 220mg stool sample were taken. Washing buffer was prepared by adding distilled water . Procedure for Purification of DNA from Stool sample: i. 220mg stool sample were collected in a 2ml tubes and placed it on ice. ii. Added 2ml Buffer ASL to each stool tube. Used pipet to wash the stool sample from the spoon while transferring the buffer. Vortexed continuously for 1minute
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Throughout the data and the observations got from this experiment‚ there are some reasons which may affected the mass of the copper was recovered and also the percentage of yield. According to the law of conservation of matter‚ the mass of the copper will not change even though there are many chemical reactions happened which also mean that the mass of copper contained in solutions or precipitates remain the same as the copper in the beginning. And it is necessary to synthesize the various copper
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The purpose of the first week experiment was to determine the effect of Nitrophenyl phosphate concentration‚ the substrate‚ on the enzyme‚ acid phosphatase‚ reaction. In an enzyme reaction‚ there is substrate that binds to the active site of the enzyme and product is the end result. The enzyme is the catalyst for the reaction which means that it speeds up the process. Without enzymes‚ the majority of reactions would not occur because the activation energy level would be unattainable. With this in
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EUROPEAN PHARMACOPOEIA 5.0 Acetylsalicylic acid TESTS Appearance of solution. Dissolve 1.0 g in 9 ml of alcohol R. The solution is clear (2.2.1) and colourless (2.2.2‚ Method II). Related substances. Examine by liquid chromatography (2.2.29). Prepare the solutions immediately before use. Test solution. Dissolve 0.10 g of the substance to be examined in acetonitrile for chromatography R and dilute to 10.0 ml with the same solvent. C. N‚N′-diacetyl-L-cystine‚ Reference solution (a).
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In this section we will analyze which steps were the most effective ones in recovering LDH (percent yield) and in purifying LDH (fold purification). As we can see looking at the Total Protein column on Table 3‚ the most effective step with regard to the percent of remaining protein removed was affinity chromatography because it was able to remove 98.6% of the remaining proteins. In comparison to 81.93% removed during the 65% ammonium sulfate precipitation and 81.3% during the size exclusion
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