Four environmental factors of enzymes were tested in lab. The changing of pH‚ substrate concentrations‚ temperature‚ and an inhibitor (NaCl) and the effects it hade on the enzyme turnip peroxidase. Enzymes are biological catalysts which increase reaction rates by lowering the activation energies of substrates. A substrate is a reactant that interacts with the enzyme. The enzyme and substrate can be viewed as the recently discovered "induced fit model"‚ which suggests enzymes are flexible and dynamic
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which can then be converted into more sugars to be used by the plant. In our experiment‚ we watch the rate of photophosphorylation‚ or the Hill Reaction‚ by using DCIP dye‚ which is blue when oxidized and colorless when reduced‚ and measuring the absorbance of a chloroplast suspension with a spectrometer. We can see how inhibitors alter the usual photosynthetic cycle and how plants evolve adaptations to deal with trying climatic conditions. ------------------------------------------------- Introduction
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measurement at 595 nm. Standard curve was prepared as shown in Table 4. Bovine serum albumin (BSA) was diluted with distilled water. The absorbance of each sample were measured using spectrophotometer at 595nm. Standard protein curve was plotted according to the concentration of protein where the x-axis and y-axis represent protein standard concentration and absorbance (595 nm) respectively. 3.10.2 Protein Determination The treated and untreated samples were measured using Bradford assay. 10µl of
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liquid Water 15mL Clear Liquid Hexane 25mL Clear liquid TABLE 2: Summary of B-Carotene Characterization Results Formula C40H56 Density 940.00 kg/m³ Melting Point 180°C) Rf value (cm/cm) 4.75/4.75=1 Absorbance at 449 nm 0.576 TABLE 3: Summary of Our Beta-carotene Sample Rf value (cm/cm) 4.75/4.75=1 Absorbance 0.186 Beers law determination of percent yield 0.00492 UV-vis spectra value Figure 1: TLC paper Figure 2: Beers law figure and calculations MEMORABLE OBSERVATIONS ANALYSIS Analysis (30):
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absorbs light in the visible region of the spectrum. It absorbs most strongly at a wavelength of 445 nm‚ I.e. it absorbs in the blue region and transmits mostly in the red region. The absorbance‚ A‚ of the solution is directly proportional to its concentration in the molarity‚ M‚ of the FeSCN2+ complex ion. Thus the absorbance obtained from the spectrophotometer can be used as a direct measure of the concentration of the FeSCN2+ ion. Equilibrium calculations Dilution: When you add water‚ or nitric
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a one centimeter path length spectrophotometer sample cell‚ and then two hundred microliters of one and six-tenths millimolar solution were pipetted into the cells as well. The absorbance was recorded every five seconds for approximately two thousand seven hundred seconds or forty-five minutes. The data for the absorbance at three hundred and seventy nanometers as well as four hundred and thirty nanometers was recorded and plotted on a scatter plot. The data was then subjected to exponential stripping
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Biological Membrane Study: HCl‚ NaOH‚ SDS Objective and Hypothesis: The objective of this lab is to determine the effects of SDS‚ HCl‚ and NaOH on red cabbage cell membrane. Prior knowledge can tell us that the red cabbage is a red-purple color due to a pigment called anthocyanin. This is what we will be testing in the experiment. We also know that HCl is a strong acid (very low pH) and that NaOH is a strong base (very high pH). From information learned in this course (lecture/lab) we can assume
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of enzyme concentration and substrate concentration on the reaction rate‚ we performed a serial dilution of enzymes to get test tubes with full‚ one-half‚ one-fourth‚ and one-eighth concentrations. We then used a spectrophotometer to get the absorbance reading over time‚ and we used these readings to determine the reaction rate. We did the same thing with a serial dilution for substrate concentration‚ and we found the reaction rate for these as well. We found that as enzyme concentration decreased
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CHEM 2303 ANALYTICAL CHEMISTRY II LECTURE 2 – APPLICATIONS OF SPECTROPHOTOMETRY TENTATIVE LECTURE SCHEDULE Date Topics • Presentation / discussion of syllabus • Tips for success • Laboratory • Introduction to the analytical process • Sample preparation Jan 9th‚ 2015 • Spectrophotometry • Properties of light • Absorption of light • Excited states • Luminescence • Applications of spectrophotometry • UV-Vis spectroscopy • Fluorimetry Jan 16th‚ 2015 • Fluorescent staining‚ green fluorescent protein
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cleaned using DI water and a kimwipe. The cuvette was then filled three-fourths full with DI water to run a blank. The absorbance was measured and the cuvette removed and cleaned. The cuvette was then filled with a saturated solution and placed in the UV-Vis. The absorbance was measured and recorded for each saturated solution in Table 2-1. This process was repeated until an absorbance for each saturated solution was
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