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5. You're studying a novel protein called Lecture Examinase. During the purification process, cells were lysed using Sodium dodecyl sulfate and beta-mercaptoethanol was added to the sample to keep Lecture Examinase functionally active. You will be performing various experiments to analyze the function of Lecture Examinase and need to know the concentration of Lecture Examinase that you've purified. A. Of the assays you leamed in the class, which assay is best suited to determine the concentration of purified Lecture Examinase? Justify your answer. ( 2 sentences max) ( 2 pts) B. Below is the absorbances you measured for the BSA standard curve. Calculate average absorbance and corrected absorbance. Mark and justify any omitted data if necessary. (2pts) C. Calculate the concentration of Lecture Examinase using the absorbances below if possible. If not, explain why you can't calculate the concentration. (2 pts) Note: a=6.6mg/ml1cm1 pathlenath =1cm D. After some testing, you find out that Lecture Examinase has the highest activity at pH 8.5. Which of the following buffers would work best in testing the enzyme function? Explain ( 1 sentence max) (2 pts) Acetate buffer (pKa 4.76) Tris buffer (pKa 8.21) Ammonia buffer (pKa 9.4) E. Using the reagents below, determine how you would make 1000mL of your buffer of choice above in 0.2M concentration at pH8.5. Show work. (2 pts) 1MAcetic acid 1M Tris base 1MAmmoniumChloride(NH4Cl) 0.5MNaOH0.5MHCl