at 595 nm. The relationship between the absorbance and concentration of the reaction was recorded on an Excel spreadsheet. RESULTS The experiment of the controls 0.2‚ 0.3‚ 0.6 and 0.9 mg/ml protein yielded optical densities of .231‚ .329‚ .645 and .970‚ respectively. Figure 1 shows a positive correlation between absorbance and concentration; as the protein concentration increased‚ so did the absorbance. Figure 1. Relationship between average absorbance and protein concentrations of 0.2‚ 0.3
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Determining the concentration of red dye #40 in an unknown solution Introduction: White light is composed of many different wavelengths of light combined together. A spectrophotometer is an instrument that shines a single wavelength of light of a known intensity into a solution and then measures the intensity of the light exiting the solution. If a solution contains
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The Beer-Lambert-Law states that there is a direct correlation between the concentration of the absorbing molecule‚ the distance the light travels‚ and the degree to which the molecules absorb light. It states that: A=a (lambda) bc (A equals total absorbance)‚ a (lambda) is the absorptive coefficient‚ b is the distance the light travels through the substance and c is the concentration. It is possible to determine the concentration of a solution using a spectrophotometer. It has two advantages: capable
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temperature would be 55 degrees Celsius and the optimal pH would be 5.5. In this experiment‚ the starch is used as a substrate to examine the optimum temperature and pH for the reaction of alpha amylase. It is known that the measuring of disappearance (absorbance) of the substrate starch with iodine using spectrophotometer will show the concentration of the substrate which will also reflect on the reaction rate. Once the reaction rates are figured out‚ the optimal temperature and pH can be determined. The
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ubility * 1 To measure the molar solubility of a sparingly soluble salt in water. * 2 To prepare a calibration curve based on complex ion formation for absorbance enhancement. * 3 To calculate the solubility product constant (Ksp) of a sparingly soluble salt from its molar solubility. * 4 To confirm the common ion effect on the molar solubility of a sparingly soluble salt. Introduction In previous introductory chemistry courses‚ you learned some basic solubility rules that are
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The anionic blue form of the dye‚ which binds to the protein‚ has a maximum absorbance of 590 nm whereas the assay reagent solution of red and green forms has a maximum absorbance of 470 nm and 650 nm. Due to the assay being sensitive with a range of 20 to 200 μg protein‚ it can be determined by the amount of dye present in the blue ionic form. This can usually be accomplished by measuring the solution at an absorbance of 595 nm. Proteins can usually be obtained from renal ultrafiltration. Proteinuria
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Abstract: Enzyme-catalyzed hydrolysis reaction occurs when an enzyme cleaves glycosidic linkage where a substrate binds to active site forming an enzyme-substrate complex. By adding water to the enzyme-substrate complex‚ products are release. One of the main factor that effect enzyme-catalyzed reactions is temperature. After an enzyme reaches an optimal temperature‚ the enzyme will result in irreversible denaturation. The irreversible denaturation causes the protein to loose its function making
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Again by observing changes in the color and by monitoring the absorbance of the system resulting from placing a stress on the system we can monitor the equilibrium of the system. For each of the two systems you will make observations of the results from stresses placed on each system‚ and use the information you collect
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concentration of an unknown solution of potassium permanganate. INTRODUCTION: UV Spectrophotometer has 4 main components which is the UV light source‚ the sample‚ detector and the processor/recorder. Spectrophotometry is a technique that uses the absorbance of light by an analyte (the substance to be analyzed) at a certain wavelength to determine the analyte concentration. Useful wavelengths for spectrophotometry range from 185 to 3‚000 nm. Spectroscopy is one of the most powerful analytical techniques
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method is utilized to monitor the enzymatic activity of invertase. Invertase was subjected to different pH (3.87‚ 4.0‚ 5.5‚ 7.3 and 10.55) of buffer solution and was observed under 540 nm absorbance using spectrophotometer. After observation and analysis‚ a peak (optimum pH) was observed by plotting absorbance versus pH. INTRODUCTION Enzymes are proteinaceous catalysts‚ which speed up the rate of a biochemical reaction. They reduce the activation energy that is essential for starting any type
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