Effects of Temperature‚ pH‚ Boiling‚ and Hydroxylamine on the Enzyme Peroxidase Extracted From Brassica rapa Abstract In this experiment the enzyme peroxidase was extracted from from a turnip‚ Brassica rapa‚ and tested under different conditions. The effects of temperature‚ boiling‚ pH‚ and a competitive inhibitor were tested. The enzyme was tested at temperatures of 4°C‚ 24°C‚ 32°C‚ and 48°C. As the temperature increased‚ so did the activity of the enzyme
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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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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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Cell Lab Report Experiments : 1. PCR . 2. Protein extraction and purification . 3. Protein concentration determination . 4. SDS-PAGE . 1. The aim of experiments : 2.1 The aim of PCR experiment is to replicate some DNA dimmers by using specific enzymes used for replication in vitro which is done in lab not by living organisms. 2.2 The aim of protein extraction and purification experiment is to extract some proteins and purify them by specific methods.
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Plot absorbance (vertical axis) against concentration of p‐nitrophenol (horizontal axis). Determination of Activation Energy of the Reaction Determination of Activation Energy of the Reaction Add 0.6 mL of enzyme solution to the reaction tubes and mix Determination of Activation Energy of the Reaction Add 0.6 mL of enzyme solution to the reaction tubes and mix Take 1 mL samples at given time points & add to tubes containing 2 mL of 0.05 M NaOH Measure absorbance against calibration blank from the calibration curve
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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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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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Objectives 1 1. To prepare a standard curve of absorbance versus protein concentration by using Bovine Serum Albumin (BSA). 2. To determine BSA concentration in two sample solutions. 3. To determine protein concentration in apple juice. Introduction What is Bradford protein assay? The Bradford protein assay is a spectroscopic analytical procedure used to measure the concentration of protein in a solution [1]. There are several reagents that can be used to determine the concentration
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adenosine triphosphate‚ also known as ATP. In order to analyze unknown glucose levels‚ a DNS assay was performed. By using 2-hydroxy-3‚5-dinitrobenzoic acid to oxidize the aldehyde group on the carbohydrate‚ the reducing end of glucose increases in absorbance of 540 nm. Using a UV spectrophotometer‚ the concentration was calculated by using a regression line of the standard curve. The experimental data concluded a 1068.912 µg/ml. With the actual concentration being 1200.000 µg/ml‚ a 10.924% error
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