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. skirt 2 – liquidation Coefficient for bovine serum albumin (BSA) pursue the UV Direct manner 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 circuit board 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 mulish using the Lowry mode. The standard curve for from each one protein was plotted, as indicated in trope 3. The BSA pr otein had a linear line whereas the lysozyme had a multinomial line. Generally, lysozyme had higher absorption values than BSA. C. plug-in 4 – Dilutions of each test protein with the Coomassie Blue method skirt 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 cant over of the line and using the Beer-Lambert practice of 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 t he diluted solution by the dilution ! mover (5): Stock Concentration2 = 0.0992...If you privation to get a full essay, pose it on our website: BestEssayCheap.com

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