Quantification Of Proteins In Solution By Spectrophotometry

Experiment 2 Quantification of Proteins in Solution by Spectrophotometry Megan downwind 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. sink 2 – liquidation Coefficient for bovine serum albumin (BSA) lease the UV Direct rule acting 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 accede 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 relentless using the Lowry method. The standard curve for to each one protein was plotted, as indicated in trope 3. The BSA p rotein had a linear line whereas the lysozyme had a multinomial line. Generally, lysozyme had higher absorption values than BSA. C.

shelve 4 – Dilutions of each test protein with the Coomassie Blue method tabularise 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 ramp of the line and using the Beer-Lambert re ctitude 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 portion (5): Stock Concentration2 = 0.0992...If you privation to get a full essay, articulate it on our website: BestEssayCheap.com

If you want to get a full essay, visit our page: cheap essay