Quantification Of Proteins In Solution By Spectrophotometry

Experiment 2
Quantification of Proteins in Solution by Spectrophotometry
Megan lee 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) employ the UV Direct Method
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
Table 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 unyielding using the Lowry method. 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.




Table 4 – Dilutions of each test protein with the Coomassie Blue method
Table 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 slope 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 factor (5): Stock Concentration2 = 0.0992...If you privation to get a full essay, order it on our website: Orderessay



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