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. deflect 2 – liquidation Coefficient for bovine serum albumin (BSA) take 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 slacken 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 sour using the Lowry regularity. The standard curve for individually 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.
carry over 4 – Dilutions of each test protein with the Coomassie Blue method circuit card 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 quenching coefficient by means of the tilt of the line and using the Beer-La mbert righteousness The absorban! ce 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 cistron (5): Stock Concentration2 = 0.0992...If you privation to get a full essay, point it on our website: BestEssayCheap.com
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