Protein analysis is an important biochemical measurement. One approach is to react the protein to form free ammonia and to spectrophotometrically measure the ammonia by reaction with phenol in the presence of sodium hypochlorite to form a blue product. The reactions is: A 4.37 mg sample of the protein was digested to convert the protein's nitrogen (molecular weight = 14.01 amu) to ammonia. It was then diluted to 100 mL. A 10.00 mL aliquot of the solution was removed and placed in a 50-mL volumetric flask where was treated with 5 mL of phenol and 2 mL of the sodium hypochlorite solution. The sample was then diluted to 50.00 mL and the absorbance at 625 nm was measured in a 1.00-cm-thick cuvette after 30 minutes elapsed for the reaction to reach completion. For reference, a standard solution was prepared from 0.0100 g of NH4Cl (molecular weight = 53.49 amu) dissolved in 1.00 L of water. Then 10.00 mL of this standard was pipette to a 50 mL volumetric flask and analyzed in the same manner as the protein sample. A reagent blank was also prepared using distilled water in place of the unknown. The following data was recorded: a) In using the absorbance data, you might be tempted to subtract the absorbance of the blank from the other absorbance values. Is this correct? Explain. b) Calculate the molar absorptivity of the blue product (include units). c) Determine the concentration of nitrogen in the cuvette containing the unknown protein sample. d) Calculate the weight percent of nitrogen in the protein. e) If a 1.00 mW laser was passed into the reference cuvette, what intensity would emerge?