Quantification Of Proteins In Solution By Spectrophotometry

Experiment 2 Quantification of Proteins in Solution by Spectrophotometry Megan leeward side 100764163 Monday PM Bench 13 Experiment 2 - Quantification of Proteins in Solution by Spectrophotometry Introduction absorbance = E * c * l. Results A1. For absorption of 4.0 x 10-5 M Absorbance = E c l E = Absorbance / (c l) E = 2.053 x 104L/mol/cm B2. dunk 2 – liquidation Coefficient for bovine serum albumin (BSA) exercise the UV Direct mode Absorbance = E c l E = Absorbance / (c l) E = 0.112 /(200 μg/mL x 1.1 cm) E = 5.09 x 10-4 mL/μg/cm put back 3 – Extinction Coefficient for lysozyme using the UV Direct Method Absorbance = E c l E = Absorbance / (c l) E = 2.36 x 10-3 mL/μg/cm B3. Absorbencies for different concentrations of BSA and lysozyme were obdurate using the Lowry manner. The standard curve for each protein was plotted, as indicated in trope 3. The BSA protein had a linear line whereas the lysozyme had a multinomial line. Generally, lysozyme had higher absorption values than BSA. C. control panel 4 – Dilutions of each test protein with the Coomassie Blue method gameboard 5 – Dilutions of each test protein with the UV Direct method Table 6 – Dilutions of each test protein with the Lowry method Table 7 – Summary table for quantification of test protein solutions by each of the troika assays Method B was used – calculating the extinction coefficient by means of the shift of the line and using the Beer-Lambert law The absorbance values for the 5 fold dilution were found to be 0.165 and 0.131. The slope of the BSA line in Figure 2 was found to be 0.0012. Absorbance = E c l c = Absorbance / (E * l) = 0.125 mg/mL Absorbance = E c l c = Absorbance / (E * l) = 0.0992 mg/mL Multiply the concentrations determined for the diluted solution by the dilution chemical element ! (5): Stock Concentration2 = 0.0992...If you privation to get a full essay, put it on our website: BestEssayCheap.com

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