the amount of protein could then be determined. After that‚ 14 test tubes were used to create a set of protein standards. Biuret solution was added to all 22 tubes and vortexed. Absorbance data was then collected by these protein standards using the SpectroVis Plus‚ and there was a direct relationship between absorbance
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calibration plot‚ which obeyed the Beer-Lambert Law. In order to determine the Fe (II) concentration‚ a series of solutions of known concentrations were made. The solutions were analyzed by the Ocean Optics spectrophotometer in order to determine their absorbance. The concentration of the unknown Fe (II) was determined by the “eye-ball” method from the Beer’s Law plot of the series of solutions. In this experiment‚ bipyridine method was used to measure the total iron concentration of an aqueous solution
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Cell Fractionation: Isolation of Mitochondria from Cauliflower and Determination of Specific Enzyme Kinetics Introduction Mitochondria is an organelle found in eukaryotic cells that play a role in biochemical processes such as respiration and energy production. Mitochondria even play an important role in apoptosis‚ or programmed cell death. This is achieved by disruption of electron transport‚ oxidative phosphorylation‚ and ATP production or even the release of proteins that trigger activation
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| | |Acid-Base Indicators: Spectroscopic Method of Determination of Ka | |Sahib Kaur | |
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˚C for future use. Kinetics Measurements Absorbance values were measured at 400 using a Thermo Scientific Genesys 20 spectrophotometer. Measurements were taken at 23 ˚C. The kinetic samples were created in 2 mL microcentrifuge tubes using a two-fold serial dilution. The catechol concentration of the samples ranged from 8.00 mM to 0.065 mM. Eight uninhibited samples were prepared by mixing 10 μL of extracted enzyme
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four solutions using clean‚ dry test tubes: 4x10⁻⁴M‚ 2x10⁻⁴M‚ 1x10⁻⁴M and 0.5x10⁻⁴M and measure the absorbance of each solution‚ respectively. Use a spectrometer to determine the absorbance of each sample. Cuvettes are placed in the cells. Rinse the cuvette with deionised water and then with the solution it will contain to avoid experimental error and an inaccurate reading of the absorbance. Fill cuvette to approx. 3/4. Be sure to adjust the machine to zero absorption. Note that KMnO4 has maximum
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Multiple samples with known properties can be measured and graphed‚ which then enables the same properties to be determined for the unknown samples‚ in this case the concentration‚ by interpolating the graph which depicts the relationship between the absorbance and concentration. Q 3. Based on the above information (in the prac manual) and your own thinking‚ which plant do you hypothesize will have more rubisco‚ one raised in the sun or one raised in shade? It is hypothesised that the sun raised silverbeet
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production of sugar molecules. However‚ I was only able to determine which of the Tubes experimented had the most or least sugar present‚ by color intensity. By operating a spectrophotometer‚ I was able to create a standard curve‚ which gave the absorbance values of glucose/maltose concentrations in the Tubes tested. From that‚ using the standard curve results and calculations (7.8 x 10^16) I then determined the µmoles of sugar present in each Tube. Finding that‚ in at least 2 minutes‚ enzyme amylase
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function like the body normally does and an experimental group that functions like the body would after consuming the Carb Cutter pill. Results were measured using levels of absorbance‚ the amount of light that shines through the solution‚ to determine how much starch is blocking the light shining through. The higher the absorbance levels‚ the higher the amount of starch in the solution. If there are still high amounts of starch in the solution‚ then this means that the
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Abstract Enzyme catalysis was observed in order to analyze how changes in temperature‚ pH‚ enzyme concentration‚ and substrate concentration affected an enzyme-catalyzed reaction. This experiment analyzed the rate of enzyme-catalyzed reactions and observed the correlation between catalase activity and products formed. It was found out that the rate of an enzyme-catalyzed reaction starts off rapidly‚ decreases‚ and levels off or completely stops‚ and can be further affected by environmental factors
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