Experiment 2 Quantification of Proteins in Solution by Spectrophotometry Megan lee(prenominal) 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. duck 2 – liquidation Coefficient for bovine serum albumin (BSA) charter the UV Direct system 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 inflexible using the Lowry method. The standard curve for apiece protein was plotted, as indicated in trope 3. Th e BSA protein had a linear line whereas the lysozyme had a multinomial line. Generally, lysozyme had higher absorption values than BSA. C.
skirt 4 – Dilutions of each test protein with the Coomassie Blue method bow 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 liquidation coefficient by means of the careen of the line and using the Beer-Lambert righteousn ess 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 component part (5): Stock Concentration2 = 0.0992...If you privation to get a full essay, golf-club it on our website:
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